Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A plasminogen/plasmin like substance (AHSAA-1), with affinity to lysine column was separated from DEAE-cellulose adsorbed human seminal plasma. Two forms of acidic arginine amidase with different affinities to LBTI (AHSAA-2) and aprotinin columns (AHSAA-3) were separated from the DEAE-cellulose adsorbed preparation and AHSAA-3 was identified as tissue kallikrein. Two basic arginine amidase preparations having affinity to LBTI (BHSAA-1) and aprotinin column were also separated from the CM-cellulose adsorbed human seminal plasma. Three basic arginine amidases with different molecular mass (BHSAA-2 to 4) were separated by Cellulofine GCL-2000 gel filtration from aprotinin adsorbed material and some of their properties were examined.
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PMID:Detection and separation of some arginine amidases including tissue kallikrein from human seminal plasma. 146 64

One major fraction hydrolysing arginine ester and amido derivative (major preparation) was detected and separated from human follicular fluid by Cellulofine GCL-2000 gel filtration. The best ester and amide substrates for this preparation were acetyl-glycyl-lysine methyl ester (Ac-Gly-Lys-Me) and D-valyl-L-leucyl-L-arginine-p-nitroanilide (Val-Leu-Arg-pNA), respectively. The preparation contained plasmin and plasminogen; lysine-Cellulofine adsorption and elution changed the substrate specificity of its esterolytic activity. After treatment by lysine-Cellulofine adsorption and elution, the basic and acidic arginine esterase activities of the major preparation were separated by CM- and DEAE-cellulose adsorption and elution, respectively. The substrate specificity of these two esterolytic enzyme activities differed before and after adsorption of the major preparation to the lysine affinity column.
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PMID:Detection of arginine esterase activity in human follicular fluid. 183 30