Vydelenie i kharakteristika alpha-spetsifichenykh trombinopodobnykh fermentov iz iadov shchitomordnika obyknovennogo (Agkistrodon halys halys) i shchitomordnika vostochnogo (sredneaziatskiǐ podvid Agkistrodon halys blomhoffii).

Translated title of the contribution: Isolation and characteristics of alpha-specific thrombin-like enzymes from venoms of the common pit viper (Agkistrodon halys halys) and the eastern pit viper (the central Asian subspecies Agkistrodon halys blomhoffii)

D. A. Solov'ev, Tatiana Ugarova

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Ancistron-H and Ancistron-B--two novel thrombin-like serine proteinases--have been purified 188- and 194-fold with a 95% recovery from the venoms of two Middle Asian subspecies of the pit viper--Agkistrodon halys halys and Agkistrodon halys Blomhoffii, using one-step affinity chromatography on agarose with an immobilized dye--Cibacron Blue F3GA (Blue-Sepharose 6B CL). The purified enzymes are one-chain glycoproteins with molecular masses of 34 and 29 kDa, pI of 6.6 and 6.3 and specific activities of 410 and 110 NIH units/mg protein, respectively. Their major amino acids are Gly, Val, Ser and Asp for Ancistron-H and Glu, Gly, Ser and Asp for Ancistron-B. During incubation with fibrinogen the enzymes cleave only the fibrinopeptide A from the A alpha-chain, leaving the B beta- and gamma-chains intact. Both enzymes hydrolyse arginine esters and thrombin-specific chromogenic peptide substrates, and display a weak caseinolytic activity but no fibrinolytic activity.

Original languageUndefined/Unknown
Pages (from-to)1221-1233
Number of pages13
JournalBiokhimiya
Volume58
Issue number8
StatePublished - Aug 1993
Externally publishedYes

Fingerprint

Venoms
Thrombin
Cibacron Blue F 3GA
Enzymes
Chromogenics
Fibrinopeptide A
Affinity chromatography
Molecular mass
Serine Proteases
Sepharose
Fibrinogen
Arginine
Glycoproteins
Esters
Coloring Agents
Amino Acids
Recovery
Peptides
Substrates
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Vydelenie i kharakteristika alpha-spetsifichenykh trombinopodobnykh fermentov iz iadov shchitomordnika obyknovennogo (Agkistrodon halys halys) i shchitomordnika vostochnogo (sredneaziatskiǐ podvid Agkistrodon halys blomhoffii).",
abstract = "Ancistron-H and Ancistron-B--two novel thrombin-like serine proteinases--have been purified 188- and 194-fold with a 95{\%} recovery from the venoms of two Middle Asian subspecies of the pit viper--Agkistrodon halys halys and Agkistrodon halys Blomhoffii, using one-step affinity chromatography on agarose with an immobilized dye--Cibacron Blue F3GA (Blue-Sepharose 6B CL). The purified enzymes are one-chain glycoproteins with molecular masses of 34 and 29 kDa, pI of 6.6 and 6.3 and specific activities of 410 and 110 NIH units/mg protein, respectively. Their major amino acids are Gly, Val, Ser and Asp for Ancistron-H and Glu, Gly, Ser and Asp for Ancistron-B. During incubation with fibrinogen the enzymes cleave only the fibrinopeptide A from the A alpha-chain, leaving the B beta- and gamma-chains intact. Both enzymes hydrolyse arginine esters and thrombin-specific chromogenic peptide substrates, and display a weak caseinolytic activity but no fibrinolytic activity.",
author = "Solov'ev, {D. A.} and Tatiana Ugarova",
year = "1993",
month = "8",
language = "Undefined/Unknown",
volume = "58",
pages = "1221--1233",
journal = "Biokhimiia (Moscow, Russia)",
issn = "0320-9725",
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AU - Solov'ev, D. A.

AU - Ugarova, Tatiana

PY - 1993/8

Y1 - 1993/8

N2 - Ancistron-H and Ancistron-B--two novel thrombin-like serine proteinases--have been purified 188- and 194-fold with a 95% recovery from the venoms of two Middle Asian subspecies of the pit viper--Agkistrodon halys halys and Agkistrodon halys Blomhoffii, using one-step affinity chromatography on agarose with an immobilized dye--Cibacron Blue F3GA (Blue-Sepharose 6B CL). The purified enzymes are one-chain glycoproteins with molecular masses of 34 and 29 kDa, pI of 6.6 and 6.3 and specific activities of 410 and 110 NIH units/mg protein, respectively. Their major amino acids are Gly, Val, Ser and Asp for Ancistron-H and Glu, Gly, Ser and Asp for Ancistron-B. During incubation with fibrinogen the enzymes cleave only the fibrinopeptide A from the A alpha-chain, leaving the B beta- and gamma-chains intact. Both enzymes hydrolyse arginine esters and thrombin-specific chromogenic peptide substrates, and display a weak caseinolytic activity but no fibrinolytic activity.

AB - Ancistron-H and Ancistron-B--two novel thrombin-like serine proteinases--have been purified 188- and 194-fold with a 95% recovery from the venoms of two Middle Asian subspecies of the pit viper--Agkistrodon halys halys and Agkistrodon halys Blomhoffii, using one-step affinity chromatography on agarose with an immobilized dye--Cibacron Blue F3GA (Blue-Sepharose 6B CL). The purified enzymes are one-chain glycoproteins with molecular masses of 34 and 29 kDa, pI of 6.6 and 6.3 and specific activities of 410 and 110 NIH units/mg protein, respectively. Their major amino acids are Gly, Val, Ser and Asp for Ancistron-H and Glu, Gly, Ser and Asp for Ancistron-B. During incubation with fibrinogen the enzymes cleave only the fibrinopeptide A from the A alpha-chain, leaving the B beta- and gamma-chains intact. Both enzymes hydrolyse arginine esters and thrombin-specific chromogenic peptide substrates, and display a weak caseinolytic activity but no fibrinolytic activity.

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