Studies on the extended active sites of acid proteinases.
about
The aspartic proteasesA new chromophoric substrate for penicillopepsin and other fungal aspartic proteinasesPenicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).Kinetics of action of pepsin on fluorescent peptide substratesAmino acid sensing in the gastrointestinal tract.The kinetics of hydrolysis of some synthetic substrates containing neutral hydrophilic groups by pig pepsin and chicken liver cathepsin DAcyl and amino intermediates in reactions catalysed by pig pepsin. Analysis of transpeptidation products.Effects of secondary binding by activator and inhibitor peptides on covalent intermediates of pig pepsin.Interactions of a low molecular weight inhibitor from Streptomyces sp. MBR04 with human cathepsin D: implications in mechanism of inactivation.Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion.
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P2860
Studies on the extended active sites of acid proteinases.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1974
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Studies on the extended active sites of acid proteinases.
@en
Studies on the extended active sites of acid proteinases.
@nl
type
label
Studies on the extended active sites of acid proteinases.
@en
Studies on the extended active sites of acid proteinases.
@nl
prefLabel
Studies on the extended active sites of acid proteinases.
@en
Studies on the extended active sites of acid proteinases.
@nl
P2860
P356
P1476
Studies on the extended active sites of acid proteinases.
@en
P2093
Sampath-Kumar PS
P2860
P304
P356
10.1073/PNAS.71.4.1070
P407
P577
1974-04-01T00:00:00Z