endopeptidase

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endopeptidase

 [en″do-pep´tĭ-dās]
any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein. Inhibition of the action of endopeptidases (proteases) in viruses causes formation of noninfectious particles; certain antiviral drugs work in this way (see protease inhibitors). Called also protease and proteinase.

en·do·pep·ti·dase

(en'dō-pep'ti-dās),
An enzyme that catalyzes the hydrolysis of a peptide chain at points well within the chain, not near either terminus; for example, pepsin, trypsin. Compare: exopeptidase.
Synonym(s): proteinase

endopeptidase

/en·do·pep·ti·dase/ (-pep´tĭ-dās) protease; any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein.

endopeptidase

(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

[en′dōpep′ti·dās]
Etymology: Gk, endon, within + Gk, peptein, to digest + ase, enzyme suffix
any peptidase that catalyzes the cleavage of internal peptide bonds in a polypeptide or protein. Endopeptidases are divided into subclasses on the basis of catalytic mechanism and comprise the serine endopeptidases, cysteine endopeptidases, aspartic endopeptidases, metalloendopeptidases, and other endopeptidases.

en·do·pep·ti·dase

(en'dō-pep'ti-dās)
An enzyme catalyzing the hydrolysis of a peptide chain at points well within the chain, not near termini (e.g., pepsin, trypsin).
Compare: exopeptidase

endopeptidase

or

proteinase

a type of PROTEASE (protein-splitting enzyme) that hydrolyses peptide bonds between particular amino acids located inside the chain, but not at the ends. There are three major endopeptidases in the mammalian gut: PEPSIN (stomach); TRYPSIN and CHYMOTRYPSIN (pancreas). Such enzymes are responsible for the first stage of protein digestion; other proteases called EXOPEPTIDASES complete the digestion of protein in the ILEUM.

endopeptidase

a peptidase capable of acting on any peptide linkage in a peptide chain.
References in periodicals archive ?
Although many peptides were observed in the MALDI mass spectra of each enzymatic digest of the cTnC fraction, only a small number of these peptides could be attributed to expected digest peptides from cTnC: <50% in the tryptic digest, <40% for the endoproteinase Glu-C digest, and <50% in the combined endoproteinase GluC/Lys-C digest.
2] fraction by endoproteinase Glu-C and subsequent MALDI-TOF MS analysis of the resulting peptides, we confirmed this assumption (data not shown).
Mass spectrometric analysis of the peptides resulting from endoproteinase Glu-C digestion of the [HbA.
Because antibody 15 and 16 are specifically directed against N-terminal domain, the immunoprecipitation of ~21-kDa fragments from endoproteinase Asp-N treated [sup.
4) proposed a high-level reference method based on liquid chromatography combined with electrospray ionization mass spectrometry (ESI-MS) analysis of the glycated and nonglycated N-terminal hexapeptides of the Hb [beta]-chains, which are released by enzymatic cleavage of the intact Hb molecule by endoproteinase Glu-C.
A reference method was established in which hemoglobin is cleaved into peptides by endoproteinase Glu-C.
1c] is based on electrospray ionization mass spectrometry (ESI/ MS) determination of the N-terminal residues of the Hb [beta] chains, which are released by enzymatic cleavage of the intact Hb molecule with endoproteinase Glu-C.
The released PSA was then isolated by immunosorption as described above, and the intact PSA as well as the peptides obtained by an endoproteinase Lys C digest were analyzed by MALDITOF MS and compared with PSA from seminal fluid.
The PEG component of macrosubstrates also may serve as a highly effective protecting group against exopeptidase action to assure that only endoproteinase activity is measured.