PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “PEPTIDE HYDROLASES”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 199 records · Page 11Linked to original sources
PubMed1963

Tropocollagen: significance of protease-induced alterations.

Interaction properties of tropocollagen are markedly altered by treatment with pepsin. This treatment liberates terminal or near-terminal covalently bonded peptides whose amino acid composition is strikingly different from the composition of the pepsin-resistant triple-helix body of the macromolecule. Pepsin also converts most of the beta-chains to alpha-chains. This fact indicates that the interchain link is also external to the body of the macromolecule and probably involves peptides. The role of these properties in bioregulative mechanisms is briefly discussed.

Amino Acids↗
PubMed1965

PEPTIDES ATTACHED TO THROMBIN: THEIR INFLUENCE ON PROTEOLYSIS.

During the activation of prothrombin at least two peptides are split off the molecule. These peptides become attached to thrombin, changing its proteolytic activity. Depending on the peptide adsorbed the endopeptidase activity of thrombin increases or diminishes. Acidification of thrombin by acetylation of amino groups uncovers the influence of peptides on the properties of thrombin.

Adsorption↗
PubMed1965

BITTER PEPTIDE ISOLATED FROM MILK CULTURES OF STREPTOCOCCUS CREMORIS.

Certain cultures of Streptococcus cremoris produced a bitter taste that occurred in the whey portion of milk cultures. Whey from a culture which produced bitterness was fractionated on Sephadex. The fraction in which the bitter taste was concentrated was chromatographed successively on paper with butanol-acetic acid-water (5:1:4), and then butanol-2-butanone-water (2:2:1). In each instance, the bitter component was in the most rapidly moving band that gave a positive ninhydrin test. The bitterness was observed to be caused by a peptide containing the following numbers of each amino acid: arginine, 1; glutamic acid, 2; glycine, 2; isoleucine, 2; leucine, 2; phenylalanine, 1; proline, 5; and valine, 4. N-terminal amino acids could be detected by coupling with 2,4-dinitrofluorobenzene or phenylisothiocyanate, or by hydrolysis with leucine aminopeptidase. When treated with carboxypeptidase, only leucine and valine appeared at the C-terminal end, and these were detected simultaneously.

Alanine↗
PubMed1964

STUDIES ON THE MECHANISM OF DESTRUCTION OF THE TOXIC ACTION OF WHEAT GLUTEN IN COELIAC DISEASE BY CRUDE PAPAIN.

The toxic action of wheat gluten on two patients was eliminated after predigestion of gluten by crude papain. This change is thought to be due to an enzyme which liberates ammonia from gluten. It is not thought that this particular mechanism operates in the normal intestinal cell but it is envisaged that one of the peptide bonds of the coeliac active constituent (possibly a N-glutaminyl peptide) is normally split by a specific intestinal peptidase which is defective in coeliac patients.

Amino Acids↗