United States Patent 4,780,529: Critical Claim Appraisal and US Patent Landscape

What does US 4,780,529 claim, in concrete technical terms?

US 4,780,529 claims a depyrogenation workflow for blood-derived parenteral products using an endotoxin inactivator that is derived from blood and is defined by chromatography-defined isolation properties plus functional endotoxin inactivation metrics. The claims split into two clusters: (1) a method of depyrogenating a pyrogenic blood product by adding the inactivator; and (2) manufacture/purification of the inactivator (and Factor IX complex) using a three-step chromatographic sequence.

Core method claims (claims 1-5)

Claim 1 is a method of depyrogenating a pyrogenic blood product by adding an “endotoxin inactivating amount” of a blood-derived inactivator that has four defining isolation parameters:

(a) molecular weight: about 61,000 daltons
(b) DEAE-Sephadex: endotoxin inactivator fraction elutes with ~0.2-0.3 M NaCl
(c) Cibacron-Blue-Sepharose: elutes with ~0.15-0.25 M NaCl
(d) Hydroxyapatite: elutes with ~0.1-0.25 M phosphate

Claim 2 narrows that the inactivator is in essentially pure form.

Claim 3 narrows further with a potency requirement. The inactivator must inactivate at least:

3,657 ng of S. typhosa endotoxin per mg inactivator
914 ng of S. enteritidis endotoxin per mg inactivator
974 ng of E. coli 055:B5 endotoxin per mg inactivator

Claim 4 narrows the “essentially pure” inactivator preparation: DEAE-Sephadex chromatography, immobilized chromophore blue (Cibacron-Blue) chromatography, then hydroxyapatite chromatography.

Claim 5 adds a stability constraint: the inactivator is essentially stable.

Product claims (claims 6-10)

Claim 6 is an “essentially nonpyrogenic blood product” for parenteral administration consisting essentially of:

a first blood protein, and
an essentially stable endotoxin inactivator derived from blood

Claims 7-10 recite embodiments for the first blood protein:

claim 7: immunoglobulin
claim 8: antihemophilic factor
claim 9: Factor IX
claim 10: interferon

Process claims (claim 11)

Claim 11 is a method for purifying Factor IX complex and endotoxin inactivator from plasma:

(a) DEAE-Sephadex chromatography on plasma
(b) elute endotoxin inactivator (partially purified) with ~0.2-0.3 M NaCl
(c) elute Factor IX complex with ~2 M NaCl
(d) run partially purified inactivator on Cibacron-blue Sepharose to yield a further purified inactivator
(e) run further purified inactivator on hydroxyapatite to yield essentially pure inactivator

Immediate internal risk: the claims are “identity by chromatography + function”

US 4,780,529 does not only claim a depyrogenation method. It also claims a specific blood-derived endotoxin inactivator identified by:

Physicochemical property: molecular weight about 61 kDa
Purification behavior on three adsorption media with specific elution ranges
Functional potency (ng endotoxin inactivated per mg inactivator)
Manufacturing sequence that produces that inactivator (for the essentially pure product)

This kind of claim construction creates enforceability strength when a competitor’s material matches all definitional constraints. It also creates invalidity and non-infringement opportunities if others achieve depyrogenation with a different identity (different molecular weight, different elution behavior, different potency, different stability profile) or if chromatography steps are “close” but not “within” the recited ranges.

How strong are the claim elements against prior art?

Without the specification’s full disclosure and without the prosecution history, the prior-art attack cannot be mapped claim-by-claim with precision. Still, the claim framework points to the key novelty leverage and the main vulnerabilities.

Likely novelty leverage (what competitors typically did not do in this exact way)

A strong argument for novelty would be the combination of:

deriving the inactivator from blood (not a generic detoxifying reagent), and
identifying it through a defined chromatographic signature (DEAE then Cibacron-blue then hydroxyapatite with specific elution windows), and
requiring a specific potency metric across endotoxin species, and
using it to make otherwise pyrogenic blood-derived parenterals essentially nonpyrogenic.

To the extent the art used endotoxin removal by physical methods (e.g., filtration, adsorption columns) or chemical neutralization agents (e.g., oxidation, hydrolysis, affinity treatments not derived from blood), it may not satisfy the “blood-derived endotoxin inactivator defined by MW and elution behavior” limitations.

Main vulnerabilities (where prior art can knock out the claim)

The likely attack surface is “obviousness” and “lack of inventive step” around:

using standard chromatography steps in a standard order (DEAE anion exchange, Cibacron-blue affinity/ion interaction, hydroxyapatite polishing),
characterizing elution in narrow salt/phosphate ranges, and
using broadly known endotoxin assays and potency reporting.

If earlier patents disclosed blood fractions or plasma-derived components that neutralize endotoxin and were purified using common chromatographic techniques, then the incremental narrowing to a “61 kDa” material with specific elution ranges can be argued as routine optimization.

The functional limitations in claim 3 can cut both ways:

They help distinguish from art that had endotoxin-reducing but not “quantified inactivation” in those exact ng/mg terms.
They also invite prior art attacks if similar assay systems and dose-response curves existed, or if those numeric thresholds were reachable through known fractionation and concentration.

Enforceability pressure points for claim scope

A competitor can reduce infringement risk by:

using a depyrogenation method that does not “add” an endotoxin inactivator in the claimed sense,
using an inactivator that differs by molecular weight, elution behavior, or potency,
using a different purification sequence (or additional steps) that yields a different identity than the “essentially pure” claimed inactivator, or
using an endotoxin removal strategy that treats the product directly rather than adding a blood-derived inactivator.

How does the landscape likely treat plasma-derived depyrogenation and endotoxin inactivation?

This patent’s claim set sits at the intersection of two established technology areas:

Depyrogenation of parenteral products (especially blood fractions)
Endotoxin neutralization/inactivation (often LPS-binding or catalytic neutralization)

In the US landscape, the dominant historical theme is that endotoxin control for parenterals is achieved through removal or reduction, which commonly includes chromatography (adsorbents), filtration, and/or chemical treatment. What is notable in US 4,780,529 is the emphasis on a defined blood-derived inactivator (not just an adsorption medium used to bind endotoxin). The claimed inactivator’s identity is locked via MW and chromatography elution properties, and the commercial product claims tie that inactivator into specific blood protein drug classes (immunoglobulin, antihemophilic factor, Factor IX, interferon).

Where is the “real” competitive leverage: the inactivator or the process?

US 4,780,529 provides leverage in both directions.

Product leverage

Claim 6 makes the inactivator part of a “consisting essentially of” composition for parenteral administration. That creates a route to enforcement not limited to the manufacturing method. If an accused product contains the claimed inactivator identity (as defined), it can be caught by product claims.

But “consisting essentially of” is a double-edged sword. It permits additional components that do not materially affect the basic and novel characteristics. That can create factual fights about:

whether any extra excipients or stabilizers “materially affect” the characteristics, and
whether the accused inactivator matches the claimed identity.

Process leverage

Claim 11 covers purification from plasma with a specific route and separation behavior:

DEAE-Sephadex: endotoxin inactivator in 0.2-0.3 M NaCl, Factor IX complex in ~2 M NaCl
Cibacron-blue Sepharose polishing
hydroxyapatite polishing

This claim can be infringed by a process that matches the separation scheme and endpoints, even if the final formulation differs.

Likely design-around paths

A competitor seeking to avoid US 4,780,529 typically would:

avoid adding a purified plasma-derived inactivator defined by the 61 kDa + chromatography signature, or
purify a similar functional fraction but ensure the identity is different (MW and/or chromatography response), or
adopt endotoxin removal strategies that do not depend on the inactivator being “derived from blood” and “essentially stable.”

What are the key claim construction variables that would decide infringement or invalidity?

1) “about 61,000 daltons”

This invites disputes over:

determination method (SDS-PAGE vs SEC vs mass spec),
aggregation/heterogeneity,
and acceptable tolerance.

A competitor with a closely related MW but not within “about” could argue non-infringement.

2) “elution of about X-Y M NaCl”

These windows define the fractions. For infringement:

the accused chromatography system must yield inactivator fractions that elute within the recited windows, under substantially similar operating conditions, or the claim would be hard to meet.

3) potency metrics (claim 3)

The ng endotoxin per mg inactivator values are numeric and assay-dependent. Outcomes turn on:

assay type (e.g., rabbit pyrogen test vs LAL method vs other),
endpoint definition (inactivation vs reduction),
lot-to-lot variability.

If the prior art used comparable fraction potency reporting, claim 3 can be vulnerable. If not, it is a strong differentiator.

4) “essentially pure form” and “essentially stable”

These qualifiers can create evidentiary battles:

purity defined by what method and threshold,
stability measured under what conditions and timeframe.

US patent landscape: how to map likely risk classes

A practical landscape assessment for US 4,780,529 usually separates prior art into four classes:

Blood fractionation techniques that isolate proteins and minor fractions through DEAE, Cibacron-blue, and hydroxyapatite.
Endotoxin inactivation or neutralization approaches using purified fractions, especially those derived from biological sources.
Depyrogenation of parenterals using chromatographic adsorption materials or process steps integrated into blood fraction purification.
Specific endotoxin quantification protocols that permit claim 3’s numeric thresholds to be met by known fractionation.

For investment or R&D planning, the decision question is not “does any prior art mention endotoxin control.” It is whether any prior art:

identifies a blood-derived endotoxin inactivator with an analogous 61 kDa identity and
specifies the three-step chromatography signature with the same elution ranges and
demonstrates potency metrics comparable to claim 3.

What is the competitive meaning of the Factor IX tie-in?

Claim 11 pairs Factor IX complex purification with inactivator isolation from plasma using DEAE separation behavior. That linkage matters because it embeds the inactivator within a commercial manufacturing platform for Factor IX products. A company operating Factor IX purification can potentially:

adopt the inactivator isolation steps and benefit from reduced endotoxin burdens; or
face enforcement risk if the isolated material matches US 4,780,529’s defined identity and is used as a formulation additive.

The product claims (immunoglobulin, antihemophilic factor, Factor IX, interferon) broaden the commercial field beyond Factor IX alone, implying that the same endotoxin inactivator concept applies across multiple blood-derived protein classes.

Potential litigation posture based on claim architecture

US 4,780,529 is structured to support:

infringement theories based on composition (claim 6) and/or
infringement theories based on manufacturing purification steps (claim 11) and/or
infringement theories based on defined inactivator identity (claims 1-5).

The numeric and chromatographic limitations can narrow the factual match required for infringement, but they also provide discrete “checkpoints” that are easy to test in an expert-driven claim chart.

From an invalidity standpoint, the combination of:

conventional chromatography steps, and
known endotoxin control assays, creates a plausible obviousness narrative if the prior art already described plasma fractions with endotoxin neutralizing activity and the purification steps are routine refinements.

Key Takeaways

US 4,780,529 claims a blood-derived endotoxin inactivator defined by ~61 kDa identity, three specific chromatography elution windows (DEAE, Cibacron-blue, hydroxyapatite), and numeric endotoxin potency thresholds.
The enforcement core is the defined inactivator identity plus the added-inactivator depyrogenation method, with broad product coverage for multiple blood protein drug classes.
The process claim for Factor IX ties inactivator isolation to a known commercial purification flow, raising practical exposure for Factor IX manufacturers.
The strongest claim differentiation comes from the chromatographic signature and potency numbers; the main invalidity risk is that prior art could already disclose blood fractions with endotoxin inactivation activity using routine chromatography and similar assays.

FAQs

Is US 4,780,529 primarily a depyrogenation method patent or a purification patent?
It covers both: depyrogenation by adding a defined blood-derived inactivator (claims 1-5) and isolation of that inactivator alongside Factor IX complex from plasma (claim 11).
What are the three adsorption media that define the inactivator identity in claim 1?
DEAE-Sephadex, Cibacron-Blue-Sepharose (chromophore blue), and hydroxyapatite.
Which claim includes quantified endotoxin inactivation potency values?
Claim 3, expressed as ng endotoxin inactivated per mg inactivator for S. typhosa, S. enteritidis, and E. coli 055:B5.
Do the product claims require a specific blood protein?
Yes. Claim 6 requires a “first blood protein,” and claims 7-10 specify immunoglobulin, antihemophilic factor, Factor IX, or interferon.
How does claim 11 manage separation between endotoxin inactivator and Factor IX complex?
Both originate from plasma after DEAE-Sephadex chromatography, with the inactivator eluting at ~0.2-0.3 M NaCl and Factor IX complex at ~2 M NaCl, followed by Cibacron-blue and hydroxyapatite polishing for the inactivator.

References

[1] United States Patent 4,780,529.

Title:	Isolation of an endotoxin inactivator from human plasma, and methods of use
Abstract:	An endotoxin inactivator is isolated from human plasma by anion exchange (DEAE-Sephadex), dye-affinity (Cibracron Blue-Sepharose), and adsorption (on hydroxyapatite) chromatography. The endotoxin inactivator, isolated in essentially pure form, may be used to depyrogenate clinical blood products.
Inventor(s):	Hao; Yu-Lee (Potomac, MD)
Assignee:	Biotech Research Laboratories, Inc. (Rockville, MD)
Application Number:	07/062,700
Patent Claims:	see list of patent claims
Patent landscape, scope, and claims summary:	United States Patent 4,780,529: Critical Claim Appraisal and US Patent Landscape What does US 4,780,529 claim, in concrete technical terms? US 4,780,529 claims a depyrogenation workflow for blood-derived parenteral products using an endotoxin inactivator that is derived from blood and is defined by chromatography-defined isolation properties plus functional endotoxin inactivation metrics. The claims split into two clusters: (1) a method of depyrogenating a pyrogenic blood product by adding the inactivator; and (2) manufacture/purification of the inactivator (and Factor IX complex) using a three-step chromatographic sequence. Core method claims (claims 1-5) Claim 1 is a method of depyrogenating a pyrogenic blood product by adding an “endotoxin inactivating amount” of a blood-derived inactivator that has four defining isolation parameters: (a) molecular weight: about 61,000 daltons (b) DEAE-Sephadex: endotoxin inactivator fraction elutes with ~0.2-0.3 M NaCl (c) Cibacron-Blue-Sepharose: elutes with ~0.15-0.25 M NaCl (d) Hydroxyapatite: elutes with ~0.1-0.25 M phosphate Claim 2 narrows that the inactivator is in essentially pure form. Claim 3 narrows further with a potency requirement. The inactivator must inactivate at least: 3,657 ng of S. typhosa endotoxin per mg inactivator 914 ng of S. enteritidis endotoxin per mg inactivator 974 ng of E. coli 055:B5 endotoxin per mg inactivator Claim 4 narrows the “essentially pure” inactivator preparation: DEAE-Sephadex chromatography, immobilized chromophore blue (Cibacron-Blue) chromatography, then hydroxyapatite chromatography. Claim 5 adds a stability constraint: the inactivator is essentially stable. Product claims (claims 6-10) Claim 6 is an “essentially nonpyrogenic blood product” for parenteral administration consisting essentially of: a first blood protein, and an essentially stable endotoxin inactivator derived from blood Claims 7-10 recite embodiments for the first blood protein: claim 7: immunoglobulin claim 8: antihemophilic factor claim 9: Factor IX claim 10: interferon Process claims (claim 11) Claim 11 is a method for purifying Factor IX complex and endotoxin inactivator from plasma: (a) DEAE-Sephadex chromatography on plasma (b) elute endotoxin inactivator (partially purified) with ~0.2-0.3 M NaCl (c) elute Factor IX complex with ~2 M NaCl (d) run partially purified inactivator on Cibacron-blue Sepharose to yield a further purified inactivator (e) run further purified inactivator on hydroxyapatite to yield essentially pure inactivator Immediate internal risk: the claims are “identity by chromatography + function” US 4,780,529 does not only claim a depyrogenation method. It also claims a specific blood-derived endotoxin inactivator identified by: Physicochemical property: molecular weight about 61 kDa Purification behavior on three adsorption media with specific elution ranges Functional potency (ng endotoxin inactivated per mg inactivator) Manufacturing sequence that produces that inactivator (for the essentially pure product) This kind of claim construction creates enforceability strength when a competitor’s material matches all definitional constraints. It also creates invalidity and non-infringement opportunities if others achieve depyrogenation with a different identity (different molecular weight, different elution behavior, different potency, different stability profile) or if chromatography steps are “close” but not “within” the recited ranges. How strong are the claim elements against prior art? Without the specification’s full disclosure and without the prosecution history, the prior-art attack cannot be mapped claim-by-claim with precision. Still, the claim framework points to the key novelty leverage and the main vulnerabilities. Likely novelty leverage (what competitors typically did not do in this exact way) A strong argument for novelty would be the combination of: deriving the inactivator from blood (not a generic detoxifying reagent), and identifying it through a defined chromatographic signature (DEAE then Cibacron-blue then hydroxyapatite with specific elution windows), and requiring a specific potency metric across endotoxin species, and using it to make otherwise pyrogenic blood-derived parenterals essentially nonpyrogenic. To the extent the art used endotoxin removal by physical methods (e.g., filtration, adsorption columns) or chemical neutralization agents (e.g., oxidation, hydrolysis, affinity treatments not derived from blood), it may not satisfy the “blood-derived endotoxin inactivator defined by MW and elution behavior” limitations. Main vulnerabilities (where prior art can knock out the claim) The likely attack surface is “obviousness” and “lack of inventive step” around: using standard chromatography steps in a standard order (DEAE anion exchange, Cibacron-blue affinity/ion interaction, hydroxyapatite polishing), characterizing elution in narrow salt/phosphate ranges, and using broadly known endotoxin assays and potency reporting. If earlier patents disclosed blood fractions or plasma-derived components that neutralize endotoxin and were purified using common chromatographic techniques, then the incremental narrowing to a “61 kDa” material with specific elution ranges can be argued as routine optimization. The functional limitations in claim 3 can cut both ways: They help distinguish from art that had endotoxin-reducing but not “quantified inactivation” in those exact ng/mg terms. They also invite prior art attacks if similar assay systems and dose-response curves existed, or if those numeric thresholds were reachable through known fractionation and concentration. Enforceability pressure points for claim scope A competitor can reduce infringement risk by: using a depyrogenation method that does not “add” an endotoxin inactivator in the claimed sense, using an inactivator that differs by molecular weight, elution behavior, or potency, using a different purification sequence (or additional steps) that yields a different identity than the “essentially pure” claimed inactivator, or using an endotoxin removal strategy that treats the product directly rather than adding a blood-derived inactivator. How does the landscape likely treat plasma-derived depyrogenation and endotoxin inactivation? This patent’s claim set sits at the intersection of two established technology areas: Depyrogenation of parenteral products (especially blood fractions) Endotoxin neutralization/inactivation (often LPS-binding or catalytic neutralization) In the US landscape, the dominant historical theme is that endotoxin control for parenterals is achieved through removal or reduction, which commonly includes chromatography (adsorbents), filtration, and/or chemical treatment. What is notable in US 4,780,529 is the emphasis on a defined blood-derived inactivator (not just an adsorption medium used to bind endotoxin). The claimed inactivator’s identity is locked via MW and chromatography elution properties, and the commercial product claims tie that inactivator into specific blood protein drug classes (immunoglobulin, antihemophilic factor, Factor IX, interferon). Where is the “real” competitive leverage: the inactivator or the process? US 4,780,529 provides leverage in both directions. Product leverage Claim 6 makes the inactivator part of a “consisting essentially of” composition for parenteral administration. That creates a route to enforcement not limited to the manufacturing method. If an accused product contains the claimed inactivator identity (as defined), it can be caught by product claims. But “consisting essentially of” is a double-edged sword. It permits additional components that do not materially affect the basic and novel characteristics. That can create factual fights about: whether any extra excipients or stabilizers “materially affect” the characteristics, and whether the accused inactivator matches the claimed identity. Process leverage Claim 11 covers purification from plasma with a specific route and separation behavior: DEAE-Sephadex: endotoxin inactivator in 0.2-0.3 M NaCl, Factor IX complex in ~2 M NaCl Cibacron-blue Sepharose polishing hydroxyapatite polishing This claim can be infringed by a process that matches the separation scheme and endpoints, even if the final formulation differs. Likely design-around paths A competitor seeking to avoid US 4,780,529 typically would: avoid adding a purified plasma-derived inactivator defined by the 61 kDa + chromatography signature, or purify a similar functional fraction but ensure the identity is different (MW and/or chromatography response), or adopt endotoxin removal strategies that do not depend on the inactivator being “derived from blood” and “essentially stable.” What are the key claim construction variables that would decide infringement or invalidity? 1) “about 61,000 daltons” This invites disputes over: determination method (SDS-PAGE vs SEC vs mass spec), aggregation/heterogeneity, and acceptable tolerance. A competitor with a closely related MW but not within “about” could argue non-infringement. 2) “elution of about X-Y M NaCl” These windows define the fractions. For infringement: the accused chromatography system must yield inactivator fractions that elute within the recited windows, under substantially similar operating conditions, or the claim would be hard to meet. 3) potency metrics (claim 3) The ng endotoxin per mg inactivator values are numeric and assay-dependent. Outcomes turn on: assay type (e.g., rabbit pyrogen test vs LAL method vs other), endpoint definition (inactivation vs reduction), lot-to-lot variability. If the prior art used comparable fraction potency reporting, claim 3 can be vulnerable. If not, it is a strong differentiator. 4) “essentially pure form” and “essentially stable” These qualifiers can create evidentiary battles: purity defined by what method and threshold, stability measured under what conditions and timeframe. US patent landscape: how to map likely risk classes A practical landscape assessment for US 4,780,529 usually separates prior art into four classes: Blood fractionation techniques that isolate proteins and minor fractions through DEAE, Cibacron-blue, and hydroxyapatite. Endotoxin inactivation or neutralization approaches using purified fractions, especially those derived from biological sources. Depyrogenation of parenterals using chromatographic adsorption materials or process steps integrated into blood fraction purification. Specific endotoxin quantification protocols that permit claim 3’s numeric thresholds to be met by known fractionation. For investment or R&D planning, the decision question is not “does any prior art mention endotoxin control.” It is whether any prior art: identifies a blood-derived endotoxin inactivator with an analogous 61 kDa identity and specifies the three-step chromatography signature with the same elution ranges and demonstrates potency metrics comparable to claim 3. What is the competitive meaning of the Factor IX tie-in? Claim 11 pairs Factor IX complex purification with inactivator isolation from plasma using DEAE separation behavior. That linkage matters because it embeds the inactivator within a commercial manufacturing platform for Factor IX products. A company operating Factor IX purification can potentially: adopt the inactivator isolation steps and benefit from reduced endotoxin burdens; or face enforcement risk if the isolated material matches US 4,780,529’s defined identity and is used as a formulation additive. The product claims (immunoglobulin, antihemophilic factor, Factor IX, interferon) broaden the commercial field beyond Factor IX alone, implying that the same endotoxin inactivator concept applies across multiple blood-derived protein classes. Potential litigation posture based on claim architecture US 4,780,529 is structured to support: infringement theories based on composition (claim 6) and/or infringement theories based on manufacturing purification steps (claim 11) and/or infringement theories based on defined inactivator identity (claims 1-5). The numeric and chromatographic limitations can narrow the factual match required for infringement, but they also provide discrete “checkpoints” that are easy to test in an expert-driven claim chart. From an invalidity standpoint, the combination of: conventional chromatography steps, and known endotoxin control assays, creates a plausible obviousness narrative if the prior art already described plasma fractions with endotoxin neutralizing activity and the purification steps are routine refinements. Key Takeaways US 4,780,529 claims a blood-derived endotoxin inactivator defined by ~61 kDa identity, three specific chromatography elution windows (DEAE, Cibacron-blue, hydroxyapatite), and numeric endotoxin potency thresholds. The enforcement core is the defined inactivator identity plus the added-inactivator depyrogenation method, with broad product coverage for multiple blood protein drug classes. The process claim for Factor IX ties inactivator isolation to a known commercial purification flow, raising practical exposure for Factor IX manufacturers. The strongest claim differentiation comes from the chromatographic signature and potency numbers; the main invalidity risk is that prior art could already disclose blood fractions with endotoxin inactivation activity using routine chromatography and similar assays. FAQs Is US 4,780,529 primarily a depyrogenation method patent or a purification patent? It covers both: depyrogenation by adding a defined blood-derived inactivator (claims 1-5) and isolation of that inactivator alongside Factor IX complex from plasma (claim 11). What are the three adsorption media that define the inactivator identity in claim 1? DEAE-Sephadex, Cibacron-Blue-Sepharose (chromophore blue), and hydroxyapatite. Which claim includes quantified endotoxin inactivation potency values? Claim 3, expressed as ng endotoxin inactivated per mg inactivator for S. typhosa, S. enteritidis, and E. coli 055:B5. Do the product claims require a specific blood protein? Yes. Claim 6 requires a “first blood protein,” and claims 7-10 specify immunoglobulin, antihemophilic factor, Factor IX, or interferon. How does claim 11 manage separation between endotoxin inactivator and Factor IX complex? Both originate from plasma after DEAE-Sephadex chromatography, with the inactivator eluting at ~0.2-0.3 M NaCl and Factor IX complex at ~2 M NaCl, followed by Cibacron-blue and hydroxyapatite polishing for the inactivator. References [1] United States Patent 4,780,529. More… ↓ ⤷ Start Trial

Applicant	Tradename	Biologic Ingredient	Dosage Form	BLA	Approval Date	Patent No.	Expiredate
Grifols Biologicals Llc	PROFILNINE, PROFILNINE HP, PROFILNINE HT, PROFILNINE SD	factor ix complex	For Injection	102476	July 20, 1981	4,780,529	2007-06-16
>Applicant	>Tradename	>Biologic Ingredient	>Dosage Form	>BLA	>Approval Date	>Patent No.	>Expiredate

Patent: 4,780,529

Summary for Patent: 4,780,529