The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2.

Dunn, B M; Valler, M J; Rolph, C E; Foundling, S I; Jimenez, M; Kay, J

Dunn, B M; Valler, M J; Rolph, C E; Foundling, S I; Jimenez, M; Kay, J.

Biochim Biophys Acta ; 913(2): 122-30, 1987 Jun 17.

Article in En | MEDLINE | ID: mdl-3109484

Subject(s)

Aspartic Acid Endopeptidases; Chromogenic Compounds/metabolism; Chymosin/metabolism; Endopeptidases/metabolism; Pepsin A/metabolism; Amino Acid Sequence; Animals; Binding Sites; Cattle; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Protein Conformation; Substrate Specificity; Swine

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Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Aspartic Acid Endopeptidases / Chromogenic Compounds / Chymosin / Pepsin A Limits: Animals Language: En Journal: Biochim Biophys Acta Year: 1987 Document type: Article Country of publication: Netherlands

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