Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.5 (thrombin)
 33,306 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chromatography of Crotalus adamanteus venom on CM-Sepharose, Cibacron Blue-Sepharose and Phenyl-Sepharose, followed by gel filtration on Ultrogel AcA 44, has resulted in the isolation in homogeneous condition of a metalloproteinase active on casein and hide powder azure. The proteinase has an alkaline isoelectric point, and the trivial name proteinase B ('basic proteinase') is suggested to distinguish it from previously characterized C. admanteus metalloproteinases. Proteinase B is a single chain glycoprotein containing one free sulfhydryl group and having a molecular weight of 60,000. Proteinase B was inactivated by treatment with EDTA, but exposure to phenylmethylsulfonyl fluoride had no effect on proteolytic activity. Proteinase B lacked hemorrhagic activity and did not digest chromogenic substrates specific for thrombin, plasmin or plasma kallikrein.
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PMID:Purification and partial characterization of a high molecular weight metalloproteinase from the venom of Crotalus adamanteus (eastern diamondback rattlesnake). 391 94

Covalently bound conjugates of human serum albumin and heparin were prepared as compounds which could improve the blood-compatibility of polymer surfaces either by preadsorption or by covalent coupling of the conjugates onto blood contacting surfaces. The conjugates (10-16 weight % of heparin) were obtained by a condensation reaction between albumin and heparin using 1-ethyl-3-(dimethylaminopropyl)-carbodiimide. Unreacted albumin and heparin were removed by diethyl-aminoethyl (DEAE)-cellulose and Cibacron Blue Sepharose chromatography respectively. The activity of the heparin component incorporated in the albumin-heparin conjugates (Ac) was compared with that of the heparin used for the synthesis of the conjugates (Anat) by thrombin time, inhibition of Factor Xa and the activated partial thromboplastin time (APTT) assays. The Ac/Anat ratio for the above assays was as follows: Thrombin time 1.25, Factor Xa inhibition 0.5. and APTT 0.5. Gel filtration chromatography showed broad-molecular weight distributions. The conjugates were fractionated using immobilized antithrombin III (ATIII). High ATIII and low ATIII affinity conjugate fractions showed the same behavior as ATIII fractionated heparin with respect to thrombin times and Factor Xa inhibition.
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PMID:Covalently bound conjugates of albumin and heparin: synthesis, fractionation and characterization. 683 42

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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PMID:[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)]. 839 70