Results 231 to 240 of about 60,176 (288)
A Length-Aware C-Terminal Rule for Prioritizing Short ACE-Inhibitory Peptides from Food Protein Hydrolysates. [PDF]
FoodsLi ML +5 more
europepmc +1 more source
The Impact of Acid-Free Reflux on Vocal Cord Granuloma. [PDF]
Laryngoscope Investig OtolaryngolLiu XH +7 more
europepmc +1 more source
Extraction, Identification, and Preliminary Investigation of the Antihypertensive Mechanism of ACE-Inhibitory Peptides from <i>Apocynum venetum</i> L. [PDF]
FoodsHuang H +6 more
europepmc +1 more source
A Native Nepenthesin Reactor for Improved Proteolytic Digestion of Intrinsically Disordered Proteins in Proteomics Workflows. [PDF]
ChembiochemWall C +6 more
europepmc +1 more source
Autonomous Hydrogel Actuators Programmed by Endogenous Biochemical Logic for Dual-Stage Morphing and Drug Release. [PDF]
Adv MaterLiu Y, Potthuri H, Sosnik A, Khoury LR.
europepmc +1 more source
Lost in the Vaso‐Occlusion: A Patient's Abdominal Pain Returns With a Vengeance
Pediatric Blood &Cancer, Volume 73, Issue 11, November 2026.
Dunia Hatabah +5 more
wiley +1 more source
Immobilization of pepsin on chitosan beads
Food Chemistry, 2007 In this study, chitosan beads were prepared by using a cross-linking agent and the resulting beads were employed in immobilization process. Studies on free and immobilized pepsin systems for determination of optimum temperature, optimum pH, thermal ...
Şenay Akkuş Çetinus
exaly +2 more sources
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Nature, 1967
THE Commission on Enzymes of the International Union of Biochemistry1 recommends that the highly active pepsin prepared from pig gastric mucosa2 which is presumed quantitatively to be the principal pepsin should retain the name originally given to it, pepsin A; the other pig pepsins3,4, initially called parapepsins, should be named B.
D J, Etherington, W H, Taylor
openaire +2 more sources
THE Commission on Enzymes of the International Union of Biochemistry1 recommends that the highly active pepsin prepared from pig gastric mucosa2 which is presumed quantitatively to be the principal pepsin should retain the name originally given to it, pepsin A; the other pig pepsins3,4, initially called parapepsins, should be named B.
D J, Etherington, W H, Taylor
openaire +2 more sources
The American Journal of Digestive Diseases, 1961
1. The most powerful adsorbents of pepsin are aluminum hydroxide gel and charcoal. 2. The adsorbent action of pepsin is uninfluenced by the substrate concentration and is less active at lowpH levels. When used to inactivate pepsin, the adsorbent effect of aluminum hydroxide gel is more important than thepH effect. 3.
D W, PIPER, B, FENTON
openaire +2 more sources
1. The most powerful adsorbents of pepsin are aluminum hydroxide gel and charcoal. 2. The adsorbent action of pepsin is uninfluenced by the substrate concentration and is less active at lowpH levels. When used to inactivate pepsin, the adsorbent effect of aluminum hydroxide gel is more important than thepH effect. 3.
D W, PIPER, B, FENTON
openaire +2 more sources
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967
It was shown that d iazoace ty l -D,L-nor leuc ine inactivates hog pepsin in the presence of copper ions at pH 5; moreover , one residue of the inhibitor is added to the enzyme molecule [1]. It is believed that the inhibitor es ter i f ies one of the carboxyl groups of the enzyme.
V M, Stepanov +2 more
openaire +2 more sources
It was shown that d iazoace ty l -D,L-nor leuc ine inactivates hog pepsin in the presence of copper ions at pH 5; moreover , one residue of the inhibitor is added to the enzyme molecule [1]. It is believed that the inhibitor es ter i f ies one of the carboxyl groups of the enzyme.
V M, Stepanov +2 more
openaire +2 more sources