Chromosomal assignments of genes for trypsin, chymotrypsin B, and elastase in mouse

1984 ◽  
Vol 10 (4) ◽  
pp. 377-383 ◽  
Author(s):  
N. K. Honey ◽  
A. Y. Sakaguchi ◽  
P. A. Lalley ◽  
C. Quinto ◽  
R. J. MacDonald ◽  
...  
Keyword(s):  
Chymotrypsin B

Lysosomal chymotrypsin B potentiates apoptosis via cleavage of Bid

2010 ◽  
Vol 67 (15) ◽  
pp. 2665-2678 ◽  
Author(s):  
Kai Zhao ◽  
Xingyu Zhao ◽  
Yaping Tu ◽  
Qi Miao ◽  
Dongxu Cao ◽  
...  
Keyword(s):  
Chymotrypsin B

Immobilized Bowman-Birk inhibitor for selective isolation of chymotrypsin B from bovine pancreas

1983 ◽  
Vol 269 ◽  
pp. 22-27 ◽  
Author(s):  
Anna Wilimowska-Pelc ◽  
Maciej Wieczorek ◽  
Jacek Otlewski ◽  
Jacek Leluk ◽  
Tadeusz Wilusz
Keyword(s):  
Selective Isolation ◽  
Bovine Pancreas ◽  
Chymotrypsin B

The Inhibition of chymotrypsins A4 and B with chloromethyl ketone reagents

1968 ◽  
Vol 46 (11) ◽  
pp. 1357-1370 ◽  
Author(s):  
Kenneth J. Stevenson ◽  
Lawrence B. Smillie
Keyword(s):  
Aromatic Ring ◽  
Histidine Residue ◽  
Straight Chain ◽  
Isolation And Identification ◽  
Chloromethyl Ketone ◽  
Basic Group ◽  
Chymotrypsin B ◽  
Chymotrypsin A

The inactivation of chymotrypsin A4 and B by the bifunctional reagents L-(1-tosylamido-2-phenyl) ethyl chloromethyl ketone (L-TPCK) and phenoxymethyl chloromethyl ketone (PMCK) has been investigated. The rate of inactivation of chymotrypsin A4 with both reagents as a function of pH has been shown to be dependent on a basic group of pK = 6.3–6.5. Chymotrypsin B inactivation appears to be dependent on a basic group with a somewhat lower pK. For each enzyme the reaction with both reagents is associated with the loss of a single histidine residue. By the isolation and identification of 3-carboxymethylhistidine from the alkylated and oxidized peptic histidine-57 peptides, it has been concluded that both enzymes are alkylated at the nitrogen-3 position of histidine-57 by L-TPCK and PMCK. Evidence for the submolar alkylation of methionine-192 of chymotrypsin A4 by L-TPCK, PMCK, D-(1-tosylamido-2-phenyl) ethyl chloromethyl ketone (D-TPCK), and N-methyl-L-TPCK is presented. There is no alkylation of the histidine of chymotrypsin A4 by D-TPCK or.N-methyl-L-TPCK.From a comparison of the structures of a number of reagents known to alkylate chymotrypsin A4, it has been concluded that the alkylation of methionine-192 is nonspecific and relatively independent of any defined stereochemistry of the reagent employed. To date the alkylation of histidine-57 has been shown to occur only with haloketones, and is dependent on the distance between the haloketone and the aromatic ring when the latter is present. Although the presence of an asymmetric α-carbon and acylamido group in straight-chain reagents is unnecessary for histidine alkylation, these must be of the L configuration if present.

Action of Chymotrypsin agr and Chymotrypsin B upon Several Protein Substrates

Science ◽  
1952 ◽  
Vol 115 (2987) ◽  
pp. 358-359 ◽  
Author(s):  
J. A. Ambrose ◽  
M. Laskowski
Keyword(s):  
Protein Substrates ◽  
Chymotrypsin B

scholarly journals Coated-vesicle shells, particle/chain material, and tubulin in brain synaptosomes. An electron microscope and biochemical study.

1976 ◽  
Vol 69 (3) ◽  
pp. 608-621 ◽  
Author(s):  
T Kadota ◽  
K Kadota ◽  
E G Gray
Keyword(s):  
Fine Particles ◽  
Biochemical Study ◽  
Matrix Material ◽  
High Resolution Electron Microscopy ◽  
Negative Staining ◽  
Coated Vesicle ◽  
Particle Chain ◽  
Resolution Electron ◽  
Flocculent Material ◽  
Chymotrypsin B

Coated vesicles (CVs), plain synaptic vesicles (PSVs), and nonvesicular flocculent material were isolated from synaptosomes and examined with goniometry and high-resolution electron microscopy after either negative staining or various biochemical procedures. The flocculent material (i.e. the presynaptic matrix material except CV shells) is largely composed of particulate or elongated (chainlike) structures; some of this material (here referred to as particle/chain material) is attached to PSVs. The results obtained were: (a) the proteinaceous properties of the CV coat (also referred to as CV shell) and the particle/chain material were demonstrated with chymotrypsin; (b) the CV shell, studied with various negative-staining techniques, differs from the particle/chain material since it has no 3-4-nm globular subunits and reacts differently to alkaline pH; (c) the particle/chain material consists of aggregates of 3-4-nm globular subunits, four of which yield 8-10-nm fine particles; and these particles can be further aggregated into chains 8-10 nm wide and up to 30-60 nm long showing a "hollow" core; (d) vinblastine sulfate induced ringlike or helical crystalloid precipitates closely resembling the vinblastine-induced microtubule crystals reported in the literature, but vinblastine had no effect on either the CV shell material or the particle/chain material.

scholarly journals Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease

2004 ◽  
Vol 17 (2) ◽  
pp. 127-131 ◽  
Author(s):  
B. Jelinek ◽  
J. Antal ◽  
I. Venekei ◽  
L. Graf
Keyword(s):  
Chymotrypsin B

scholarly journals Chymotrypsin B Cached in Rat Liver Lysosomes and Involved in Apoptotic Regulation through a Mitochondrial Pathway

2008 ◽  
Vol 283 (13) ◽  
pp. 8218-8228 ◽  
Author(s):  
Qi Miao ◽  
Yang Sun ◽  
Taotao Wei ◽  
Xingyu Zhao ◽  
Kai Zhao ◽  
...  
Keyword(s):  
Rat Liver ◽  
Mitochondrial Pathway ◽  
Liver Lysosomes ◽  
Chymotrypsin B ◽  
Rat Liver Lysosomes

The reaction with nitrous acid of the "active site" N-terminal isoleucine in chymotrypsin and derivatives

1970 ◽  
Vol 48 (6) ◽  
pp. 671-681 ◽  
Author(s):  
Joan W. Dixon ◽  
T. Hofmann
Keyword(s):  
Active Site ◽  
Rate Constants ◽  
Nitrous Acid ◽  
Amino Group ◽  
Amino Groups ◽  
Guanidinium Chloride ◽  
Third Order ◽  
Potential Activity ◽  
Chymotrypsin B ◽  
Nitrophenyl Ester

Bovine α-chymotrypsin, δ-chymotrypsin, homoarginine-δ-chymotrypsin, and bovine chymotrypsin B were inactivated by nitrous acid at pH 3.8–4.4 and 0°. The potential activity of bovine chymotrypsinogen A was not affected under these conditions. The inactivation rates as measured with the substrates α-N-acetyl-L-tyrosine ethyl ester, carbobenzoxyglycine p-nitrophenyl ester, and p-nitrophenyl acetate, and by 3H-di-isopropyl phosphorofluoridate incorporation were identical with the deamination rates of the amino group of the N-terminal isoleucine-16, but were slower than the deamination rates of the amino groups of the N-terminals half-cystine-1 and alanine-149. It is concluded that the deamination of isoleucine-16 is directly responsible for the inactivation. Third-order deamination rate constants of the N-terminal isoleucine-16 were measured and the following values (in min−1M−2) were obtained: α-chymotrypsin, 0.4–0.6; homoarginine-δ-chymotrypsin, 0.05; di-isopropyl phosphoryl-α-chymotrypsin, [Formula: see text]; tosyl-α-chymotrypsin, 0.05; chymotrypsin B, 0.3; α-chymotrypsin in guanidinium chloride, 30–50; homoarginine-δ-chymotrypsin in guanidinium chloride, > 20. The deamination rate constants for the model dipeptides isoleucylvaline and valylvaline are 40 and 46, respectively (Kurosky, A., and Hofmann, T.: to be published). A comparison shows that the constants for the dipeptides and the two chymotrypsins in guanidinium chloride are very close and are probably those of a fully exposed amino group. The much lower constants for the other enzymes and derivatives represent the varying degrees of accessibility of the amino group and show the usefulness of the reagent as a conformational probe. The results are fully compatible with the proposed structure of α-chymotrypsin (1) and the proposed function of the N-terminal isoleucine (2).

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