Rapid Identification of Superior Endogenous Signal Peptides for Heterologous Protein Secretion by Corynebacterium glutamicum Through Modular Cloning and Automation. [PDF]
Matamouros S +4 more
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A Comparative Analysis of Receptor-Like Kinases in Chlorophyta Reveals the Presence of Putative Cell Wall Integrity Sensors. [PDF]
Marcianò D +4 more
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Proteomic Studies for the Identification and Characterization of Marine Bioactive Molecules. [PDF]
Rosic N.
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The Current Toolbox for Covalent Inhibitors: From Hit Identification to Drug Discovery. [PDF]
You M, Liu H, Li C.
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The influence of proteolytic enzymes on the change of lysozyme properties. [PDF]
Tomczyk Ł +5 more
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Peptidylglutamyl-peptide hydrolase activity of the multicalytic proteinase complex
Hakim Djaballah
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Signal peptidases and signal peptide hydrolases
Journal of Bioenergetics and Biomembranes, 1990Signal peptidases, the endoproteases that remove the amino-terminal signal sequence from many secretory proteins, have been isolated from various sources. Seven signal peptidases have been purified, two from E. coli, two from mammalian sources, and three from mitochondrial matrix.
I K, Dev, P H, Ray
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Peptide hydrolases of Antartic krill, Euphausia superba
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985Abstract 1. 1. A survey has been made of the peptide hydrolase activities occurring in Antarctic krill, Euphausia superba. 2. 2. A major protein hydrolyzing activity in the pH range of 6–8, and a minor activity at pH 3–4, were detected. 3. 3. Temperature optima of approx.
Knut Kr. Osnes, Viggo Mohr
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Rapid colorimetric assay for intestinal peptide hydrolases
Analytical Biochemistry, 1974Abstract A simple two-step method is described for quantitating the release of free l -phenylalanine, l -leucine, l -methionine, or l -isoleucine from di- or polypeptides. The colorimetric assay is based on the ability of l -amino acid oxidase to catalyze the oxidation of free l -amino acid, but not of peptides.
C R, Shoaf +2 more
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