endopeptidase

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en·do·pep·ti·dase

 (ĕn′dō-pĕp′tĭ-dās′, -dāz′)
n.
Any of a large group of enzymes that catalyze the hydrolysis of peptide bonds in the interior of a polypeptide chain or protein molecule.

endopeptidase

(ˌɛndəʊˈpɛptɪˌdeɪz)
n
(Biochemistry) any proteolytic enzyme, such as pepsin, that splits a protein into smaller peptide fragments. Also called: proteinase Compare exopeptidase
Translations
endoprotéase
References in periodicals archive ?
Alcalase, an endoproteinase, can hydrolyze proteins to peptides possessing hydrophobic amino acids at the end of their peptide chains.
Lethal factor (LF) toxemia was quantified at CDC's Clinical Chemistry Branch, Division of Laboratory Sciences (Atlanta, GA, USA), by using a validated mass spectrometry method that reports specific LF endoproteinase activity in nanograms per milliliter of serum.
20) Briefly, the protein pellets left after RNA isolation were reconstituted, reduced with Tris(2-carboxyethyl)phosphine, and digested successively with cyanogen bromide, endoproteinase Lys-C, and trypsin.
5 mg) was reduced by dithiothreitol, S-carbox-amidom ethylated and digested with endoproteinase C (substrate:enzyme = 50:1, w/w) in 40 [micro]l of 10 mM Tris- HCl (pH 7.
Peptide mapping and evaluation of glycopeptide microheterogeneity derived from endoproteinase digestion of erythropoietin by affinity high-performance capillary electrophoresis.
Next, the hemolysate is incubated with the endoproteinase Glu-C for 18 hours at 37[degrees]C to cleave Hb into peptides, whereby the specific glycated and non-glycated N-terminal peptides of the [beta]-chain of Hb are measured by either capillary electrophoresis or electrospray ionization mass spectrometry.
Amin I, Jinap S, Jamilah B (1998) Proteolytic activity (aspartic endoproteinase and carboxypeptidase) of cocoa bean during fermentation.
4]-labeled sample was then subjected to proteolytic digestion with endoproteinase Asp-N, which cleaves at aspartic acid residues, or aminopeptidase I, which nonspecifically removes amino acid residues inwards from N-terminus, for I hour at room temperature and followed by immunoprecipitation.
95 units of carboxypeptidase B (Sigma), 2 units of endoproteinase glu-C (Boehringer-Mannheim), or 1.
In brief, the N-terminal hexapeptide of the hemoglobin [beta] chain is enzymatically cleaved by the proteolytic enzyme endoproteinase Glu-C before analysis.
LF endoproteinase activity was quantified by using mass spectrometry (3).