What question did this study set out to answer?

To isolate and characterize the heat-labile plasma clotting agent variously known as accelerator globulin, proaccelerin, or Factor V.

January 1, 1956Journal of Clinical InvestigationOpen Access

Chromatographic Purification of Human Serum Accelerator Globulin 1

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Authors

FCFrederick M. CoxLAC+USC Medical Center GLGerard F. LanchantinUniversity of Southern California AWArnold G. WareThe University of Texas Southwestern Medical Center

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Implication

Biochemical analysis demonstrates isolation of heat-labile accelerator globulin from human plasma, indicating its role in correcting prolonged prothrombin time.

Key Points

To isolate and characterize the heat-labile plasma clotting agent variously known as accelerator globulin, proaccelerin, or Factor V.
Assayed human plasma fractions for prothrombin-converting accelerator activity.
Tested protein adsorption characteristics using barium sulfate suspensions.
Evaluated corrective effects on prothrombin times using aged, oxalated human plasma.
Confirmed the clotting agent is a protein that potentiates thromboplastin activity during prothrombin conversion.
Demonstrated that the active factor does not adsorb onto barium sulfate.
Observed complete correction of prolonged prothrombin times when adding the factor to aged oxalated human plasma.

Cite This Study

Cox et al. (1956) studied this question.

synapsesocial.com/papers/6a8508a680907ad94f0cc463 https://doi.org/10.1172/jci103243

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Implication

Biochemical analysis demonstrates isolation of heat-labile accelerator globulin from human plasma, indicating its role in correcting prolonged prothrombin time.

Chromatographic Purification of Human Serum Accelerator Globulin 1

Discussion

Member takes

Implication

Key Points

Cite This Study

Chromatographic Purification of Human Serum Accelerator Globulin 1

Discussion

Member takes

Implication

Key Points

Cite This Study

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