THE RESISTANCE OF α-AMYLASES TOWARDS PROTEOLYTIC ATTACK
نویسندگان
چکیده
منابع مشابه
Glycosylation and secretion of human α-amylases
Three human α-amylases exist: Amy1 (salivary amylase), Amy2A (pancreatic amylase), and Amy2B (expressed in various tissues). These amylases share a 97% 99% amino acid sequence identity, and two potential N-glycosylation sites (N427 and N476) are commonly found in the C-terminal region. In general, salivary amylase is more frequently glycosylated than pancreatic amylase, and it is still uncertai...
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Inhibition of Sunn Pest, Eurygaster integriceps, α-Amylases by α-Amylase Inhibitors (T-αAI) from Triticale
The effect of triticale α-amylases inhibitors on starch hydrolysis catalyzed by the Sunn pest, Eurygaster integriceps Puton (Hemiptera: Scutelleridae) midgut amylases was examined. Biochemical studgawies showed that inhibitors from Triticale (a hybrid of wheat and rye) had inhibitiory effects on E. integriceps α-amylases. The effects of the triticale α-amylase inhibitor (T-αAI) on α-amylase of ...
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Electrostatic interactions are of vital importance in diverse aspects of protein structure and function [1-5], including the catalytic activity [6,7], ligand binding [8], complex formation [9], proton transport [10,11], as well as their stability of folded proteins [12,13]. These interactions involve full charges on the side chains of ionizable amino acids that arise from the association and di...
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Transient starch in leaves is synthesized by various biosynthetic enzymes in the chloroplasts during the light period. This paper presents the first mathematical model for the (bio)synthesis of the chain-length distribution (CLD) of transient starch to aid the understanding of this synthesis. The model expresses the rate of change of the CLD in terms of the actions of the enzymes involved. Usin...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1958
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77406-7