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Journal of the Korean Chemical Society (JKCS)

ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 14, Number 2
JKCSEZ 14(2)
April 20, 1970

Title	The Kinetics of the Pepsin-Catalyzed Hydrolysis of N-Carbobenzoxy-L-Glutamyl-L-Tyrosine by Determination of the Spectrophotometer 합성기질 N-Carbobenzoxy-L-glutamyl-L-tyrosine의 Pepsin 가수분해반응의 분광광도법에 의한 속도론적 연구
Author	Hong Dae Shin 신홍대
Keywords
Abstract	The kinetics of the pepsin-catalyzed hydrolysis of N-carbobenzoxy-L-glutamyl-L-tyrosine at pH 3.5 and 37℃ were determined by a spectrophotometric technique. The pepsin used was further purified on a Sephadex G-75 column. The kinetics data were Km = l.7 × 10-3M, -ΔF°= 3.99Kcal/mole, and k3= 2.1 × 10-2sec-1. An analysis of the above data and other investigators' data obtained from some dipeptides led to the following conclusions. (1) Phenylalanyl residues in a synthetic peptide are bound to pepsin more strongly than glutamyl or tyrosyl residues, supporting the theory that a part of the binding region of the active center is hydrophobic. (2) Dipeptides are bound to pepsin principally through their side chains and the binding involves both side-chain residues. (3) The nature of amino acids in dipeptides R2-R1, affect the k3 values.
Page	155 - 160
Full Text	PDF

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