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 ?
To identify additional glycosylation sites, single (trypsin) and double (trypsin combined with endoproteinase Glu-C) protease digestions of partially deglycosylated TIP samples were analyzed by nano-LC ESI-[MS.
We found that adding additional endoproteinase Glu-C was crucial to ensure complete proteolysis [125 [micro]g/ mg hemoglobin vs the reported amount of 10 [micro]g (2)].
2] terminus of cTnT is rich in glutamic acid residues, which produces very small peptides when digested with endoproteinase Glu-C, and low in lysine and arginine residues, which produces very large peptides when digested with trypsin or endoproteinase Lys-C.
These peaks may represent activity of an endoproteinase followed by an N-terminal exopeptidase, i.
Globin chains were digested by adding 1 [micro]g of endoproteinase Glu-C (Boehringer Mannheim) or 0.
In the reference method, hemoglobin is cleaved by endoproteinase Glu-C.
The first step in the procedure for the IFCC reference method (specifically measuring the [beta]-N-terminal hexapeptide) is the cleavage of hemoglobin with the proteolytic enzyme endoproteinase Glu-C at position 6 from the N-terminal end of the ([beta]-chain.
In the first step, Hb from washed and lysed erythrocytes is cleaved into peptides by the proteolytic enzyme endoproteinase Glu-C.
A reference method was established in which hemoglobin is cleaved into peptides by endoproteinase Glu-C.
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.