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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

LOC618826 chymotrypsinogen B1-like

Top mentioned proteins: Trypsin, ACID, HAD, CAN, elastase
Papers on Chymotrypsin
The modifier effects of chymotrypsin and trypsin enzymes on fluorescence lifetime distribution of "N-(1-pyrenyl)maleimide-bovine serum albumin" complex.
Pekcan et al., İstanbul, Turkey. In Spectrochim Acta A Mol Biomol Spectrosc, Mar 2016
Chymotrypsin and trypsin are the well known proteolytic enzymes, both of which are synthesized in the pancreas as their precursors - the inactive forms; chymotrypsinogen and trypsinogen - and then are released into the duodenum to cut proteins into smaller peptides.
An Investigation into the Gastrointestinal Stability of Exenatide in the Presence of Pure Enzymes, Everted Intestinal Rings and Intestinal Homogenates.
Kong et al., Jilin, China. In Biol Pharm Bull, Dec 2015
Chymotrypsin showed the greatest ability to degrade exenatide (half-life t1/2, 5.784×10(-2) h), whereas aminopeptidase N and carboxylpeptidase A gave t1/2 values of 3.53 and 10.16 h, respectively.
Synthesis of the kyotorphin precursor benzoyl-L-tyrosine-L-argininamide with immobilized α-chymotrypsin in sequential batch with enzyme reactivation.
Guzmán et al., Valparaíso, Chile. In Biotechnol Prog, Nov 2015
UNASSIGNED: α-Chymotrypsin was immobilized in activated agarose support and the stability of the biocatalyst was assessed in three polar organic solvents, namely, ethanol, diglyme, and acetonitrile.
Isolation and Identification of Dipeptidyl Peptidase IV-Inhibitory Peptides from Trypsin/Chymotrypsin-Treated Goat Milk Casein Hydrolysates by 2D-TLC and LC-MS/MS.
Chen et al., Beijing, China. In J Agric Food Chem, Nov 2015
New dipeptidyl peptidase IV (DPP-IV)-inhibitory peptides from trypsin/chymotrypsin-treated goat milk casein hydrolysates were isolated and identified by two-dimensional silica thin-layer chromatography (2D-TLC) combined to nano LC-MS/MS.
[Preliminary Genetic and Functional Analyses of Schistosoma japonicum Chymotrypsin-like Protease].
Hu et al., In Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi, Aug 2015
OBJECTIVE: To investigate the gene expression, localization and potential functions of Schistosoma japonicum chymotrypsin-like protease (SjCTRL) in the host, and evaluate its potential immune-protection efficacy against S. japonicum infection in mice.
NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
Song et al., Singapore, Singapore. In Plos One, 2014
Here as facilitated by our previous discovery, the isolated NS3pro has been surprisingly deciphered by NMR to be the first intrinsically-disordered chymotrypsin-like fold, which exists in a loosely-packed state with non-native long-range interactions as revealed by paramagnetic relaxation enhancement (PRE).
Treatment and mechanism of BMMSCs on deep II degree scald of hamster skin.
Tuhan et al., Ürümqi, China. In Genet Mol Res, 2014
Polymerase chain reaction was used to detect the amount of chymotrypsin in mast cells.
Effect of High Pressure on the Porcine Placenral Hydrolyzing Activity of Pepsin, Trypsin and Chymotrypsin.
Hong et al., Seoul, South Korea. In Korean J Food Sci Anim Resour, 2013
This study investigated the effects of protease treatments (trypsin, chymotrypsin, and pepsin) under various pressure levels (0.1-300 MPa) for the characteristics of porcine placenta hydrolysates.
Effects of Concentration and Reaction Time of Trypsin, Pepsin, and Chymotrypsin on the Hydrolysis Efficiency of Porcine Placenta.
Hong et al., Seoul, South Korea. In Korean J Food Sci Anim Resour, 2013
This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates.
Chymotrypsin C mutations in chronic pancreatitis.
Sahin-Tóth et al., Boston, United States. In J Gastroenterol Hepatol, 2011
Mutations in the chymotrypsin C (CTRC) gene encoding the digestive enzyme CTRC have been shown to increase the risk of chronic pancreatitis in European and Asian populations.
Genetics of pancreatitis: a guide for clinicians.
Witt, München, Germany. In Dig Dis, 2009
Chymotrypsin C (CTRC) degrades all human trypsin isoforms with high specificity.
Chymotrypsin-poly vinyl sulfonate interaction studied by dynamic light scattering and turbidimetric approaches.
Farruggia et al., Rosario, Argentina. In Biochim Biophys Acta, 2008
The formation of non-soluble complexes between a positively charged protein and a strong anionic polyelectrolyte, chymotrypsin, and poly vinyl sulfonate, respectively, was studied under different experimental conditions.
Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis.
Sahin-Tóth et al., Leipzig, Germany. In Nat Genet, 2008
Here we have analyzed the gene encoding the trypsin-degrading enzyme chymotrypsin C (CTRC) in German subjects with idiopathic or hereditary chronic pancreatitis.
Ultrafast surface hydration dynamics and expression of protein functionality: alpha -Chymotrypsin.
Zewail et al., Pasadena, United States. In Proc Natl Acad Sci U S A, 2002
report studies of hydration dynamics at the surface of bovine pancreatic alpha-chymotrypsin
Trypsin: a case study in the structural determinants of enzyme specificity.
Hedstrom, Waltham, United States. In Biol Chem, 1996
Trypsin and chymotrypsin have similar tertiary structures, although very different substrate specificities.
[Cytokeratins as markers of differentiation. Expression profiles in epithelia and epithelial tumors].
Moll, Mainz, Germany. In Veroff Pathol, 1992
Chymotrypsin-cleaving experiments revealed the presence of a resistant core fragment (M(r) 38,000), indicating a alpha-helical "coiled-coil" conformation typical of IFs.(ABSTRACT TRUNCATED AT 400 WORDS)
Structure and function of a calmodulin-dependent smooth muscle myosin light chain kinase.
Bailin, In Experientia, 1984
Chymotrypsin digestion of the kinase from smooth muscle generates a fragment of Mr 80,000 that does not contain the calmodulin binding or cyclic AMP-dependent protein kinase phosphorylation sites.
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