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Intestinal surface peptide hydrolases: identification and characterization of three enzymes from rat brush border.

Abstract:

Peptide hydrolases were solubilized from rat small intestinal brush border by papain and separated by Sephadex G-200 chromatography, velocity gradient ultracentrifugation and polyacrylamide disc electrophoresis and designated according to approximate molecular size from sedimentation studies. Peptidases I (apparent Mr 230 000) and II (apparent Mr 160 000) are oligopeptidases with maximum specificity for tripeptides with identical pH optima (7.5) and similar apparent Km with L-Leu-Gly (I, 0.60...

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Publication status:
Published

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Authors


Wojnarowska, F More by this author
Journal:
Biochimica et biophysica acta
Volume:
403
Issue:
1
Pages:
147-160
Publication date:
1975-09-05
DOI:
ISSN:
0006-3002
URN:
uuid:311ba14c-5ee7-4d90-a2d0-d68702702e8f
Source identifiers:
22729
Local pid:
pubs:22729

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