What question did this study set out to answer?

To determine the specific proteolytic action of Arvin enzyme preparations derived from Agkistrodon rhodostoma venom on human fibrinogen.

July 1, 1970Biochemical JournalOpen Access

The proteolytic action of Arvin on human fibrinogen

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Authors

MEM. R. EwartWren Laboratories (United States)MHM.W.C. HattonMcMaster University Medical Centre JBJohn M. BasfordUniversity of Wales

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Implication

Biochemical analysis reveals selective cleavage of fibrinopeptides AP, AY, and A from human fibrinogen by Arvin, highlighting its distinct mechanism from other clotting enzymes.

Key Points

To determine the specific proteolytic action of Arvin enzyme preparations derived from Agkistrodon rhodostoma venom on human fibrinogen.
Digested human fibrinogen with two enzyme preparations from Agkistrodon rhodostoma venom: purified IRC-50 Arvin and less purified clinical Arvin.
Isolated and identified the specific peptide fragments released during the proteolytic reaction.
IRC-50 Arvin selectively liberated three peptides identified as fibrinopeptides AP, AY, and A, while releasing no fibrinopeptide B.
Clinical Arvin released fibrinopeptides AP, AY, and A alongside small amounts of two derivative heptapeptides, reflecting contamination by an additional enzyme.
The peptide liberation pattern of Arvin mirrored that of reptilase, despite Arvin's inability to activate fibrin-stabilizing factor.

Cite This Study

Ewart et al. (1970) studied this question.

synapsesocial.com/papers/6a85c068b451cea71dae79f3 https://doi.org/10.1042/bj1180603

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Implication

Biochemical analysis reveals selective cleavage of fibrinopeptides AP, AY, and A from human fibrinogen by Arvin, highlighting its distinct mechanism from other clotting enzymes.

The proteolytic action of Arvin on human fibrinogen

Discussion

Member takes

Implication

Key Points

Cite This Study

The proteolytic action of Arvin on human fibrinogen

Discussion

Member takes

Implication

Key Points

Cite This Study

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