Cysteine proteinase of Entamoeba histolytica. II. Identification of the major split position in bovine insulin B-chain.
The substrate specificity of a cysteine proteinase of Entamoeba histolytica was tested using the oxidized B-chain of bovine insulin. 28 proteolytic peptides were formed after different intervals of incubation and could be separated by high-performance liquid chromatography. Two dominant peptides appearing after 10 min of incubation were isolated and analyzed for amino acid composition. The results obtained indicate that these two peptides were formed by cleavage of the peptide bond between the amino acids 23 and 24. Thus as major split position the Gly-Phe bond in the insulin B-chain could be identified.
Scholze
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H
Otte
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Werries
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D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D004748:Entamoeba histolytica / Q000201:enzymology*; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism*; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D013379:Substrate Specificity
D000596:Amino Acids; D007328:Insulin; D010455:Peptides; D010450:Endopeptidases; D003546:Cysteine Endopeptidases