Currently, the term "peptidase" is also used equivalently with "protease" and "proteinase." Peptidase was restricted to the enzymes included in subsubclasses EC 3.4.11-19, the
exopeptidases in the Enzyme Nomenclature (1984), while the term "proteinases" was previously used for the enzymes included in subsubclasses EC 3.4.21-99 having the same meaning as "endopeptidase." However, the terms "protease" and "proteinase" are still preferred by many scientists [3].
Addition of plant protein hydrolysates into the medium without FBS had shown a slight improvement in the cell growth (cell died after 4 to 5 days) with hydrolysates from Alcalase for both soybean and rice hydrolysates (Figure 2A and 2B).The protein extracts by Flavourzyme as an
exopeptidase did not have significant effect on cell culture.
Non-proteasome proteases have been divided into
exopeptidases and endopeptidases depending on the cleavage position of target proteins.
DPP-4 is a serine
exopeptidase hormone, known to degrade two major gut incretin hormones that stimulate insulin release, that is, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), leading to a very short half-life (approximately 2 min) of the hormones [58-61].
CatB is considered a major lysosomal cysteine protease for the degradation of collagen in soft connective tissues, as it possesses both endopeptidase and
exopeptidase activity which differs from other lysosomal cysteine proteases [44].
It was only later revealed that most serum peptides sort into nested sets of sequences, generated by
exopeptidase activities superimposed on the proteolytic events of the ex vivo coagulation and complement degradation pathways (3), thus explaining the erratic measurements when preanalytical conditions are not exceedingly well controlled.
This enzyme is an
exopeptidase with endopeptidase and glutaminase side activities.
This is a protease preparation containing endo-,
exopeptidase and glutaminase that can be used to hydrolyse proteins such as wheat and soya.
Multiple molecular forms of serum amyloid A, related to trimming of the peptide chain by
exopeptidase, have been noted by MALDI- or SELDI-TOF MS (30, 46-50).
The
exopeptidase dipeptidyl-peptidase IV (DPP IV/CD26; EC 3.4.14.5), a cell-surface protease that occurs in a soluble form in plasma, cleaves many bioactive peptides of medical importance.
The identity of target glycopeptides was further confirmed through controlled digestion with
exopeptidase and exoglycosidase.
These peaks may represent activity of an endoproteinase followed by an N-terminal
exopeptidase, i.e., an aminopeptidase, with profiles changing with time in plasma and serum.
