Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The differential cleavage of surface proteins of Borrelia burgdorferi IRS strains by several proteases was examined. Proteinase K, trypsin, chymotrypsin and thermolysin all cleaved the outer surface protein B (OspB) to undetectable levels by Coomassie Brilliant Blue staining, whereas some residual protein was detected by immunoblotting with polyclonal and monoclonal antibodies. Not even antigenic fragments were detectable by immunoblotting with 1A8 monoclonal antibody reactive with OspB. Less effective or ineffective was the cleavage of OspB by V8 protease and proteinase A, respectively. The outer surface protein A was cleaved only by proteinase K. The effect of trypsin on borreliae viability and adhesion to cultured cells was also studied. The trypsin treatment of borreliae did not impair the viability of organisms which continued to synthesize the cleaved OspB. The attachment of B. burgdorferi to HEp-2 cells was reduced by 41% after treatment with trypsin, whereas preincubation of borreliae with monoclonal antibody 1A8 and guinea pig immune serum reduced the adhesion of borreliae to the cells by 32% and 87%, respectively.
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PMID:Differential cleavage of surface proteins of Borrelia burgdorferi by proteases. 160 94

The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli, has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, ASN3, Thr4, Ser3, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile9, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.
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PMID:The primary structure of Bacillus subtilis acidic ribonsomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence. 677 Dec 49

The complete covalent structure of Protein B, the third major protein degraded during germination of Bacillus megaterium spores, has been determined. The intact protein was cleaved with the specific B. megaterium spore protease into three peptides, residues 1 to 31 (B-III), 32 to 66 (B-I), and 67 to 96 (B-II). Cleavage of the intact protein with trypsin allowed isolation of the peptide encompassing residues 61 to 77 (T-11) as well as the COOH-terminal peptide, residues 94 to 96 (T-4). Cleavage of Peptide B-I with trypsin or chymotrypsin allowed isolation of peptides encompassing residues 53 to 60 (B-I-T-2) and residues 52 to 66 (B-I-C-4), respectively. Subtractive Edman degradation of Peptide T-4, automated sequenator analysis of Peptides B-I, B-II, T-11, B-I-T-2, and B-I-C-4, previously published partial sequence data on the intact B-protein and carboxypeptidase V digestion of the intact protein provided the data from which the following unique sequence was deduced: NH2-Ala-Lys-Gln-Thr-Asn-Lys-Thr-Ala-Ser-Gly-Thr-Ser-Thr-Gln-His-15 Val-Lys-Gln-Gln-Asp-Ala-Gln-Ala-Ser-Lys-Asn-Asn-Phe-Gly-Thr-30 Glu-Phe-Gly-Ser-Glu-Thr-Asn-Val-Gln-Glu-Val-Lys-Gln-Gln-Asn-45 Ala-Gln-Ala-Ala-Asn-Lys-Ser-Gln-Asn-Ala-Gln-Ala-Ser-Lys-60 Asn-Asn-Phe-Gly-Thr-Glu-Phe-Ala-Ser-Glu-Thr-Ser-Ala-Gln-Glu-75 Val-Arg-Gln-Gln-Asn-Ala-Gln-Ala-Gln-Lys-Lys-Asn-Gln-Asn-90 Ser-Gly-Lys-Tyr-Gln-Gly-COOH. The primary sequence of the B-protein contains a large internal duplication (residues 17 to 50 and 52 to 85), and shows significant sequence homology with the A- and C-proteins, the other major proteins degraded during B. megaterium spore germination.
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PMID:The complete covalent structure of protein B. The third major protein degraded during germination of Bacillus megaterium spores. 677 16

We investigate the average inter-residue folding forces derived from mutational data of the 15 proteins: barstar, barnase, chymotrypsin inhibitor 2 (CI2), Src SH3 domain, spectrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7 (IM7), colicin E9 immunity protein 9 (IM9), spectrin R17 domain, and ubiquitin. The residue-specific contributions to folding in most of the 15 protein molecules are highly non-uniformly distributed and are typically about 1piconewton (pN) per interaction. The strongest folding forces often occur in some of the helices and strands of folding nuclei which suggests that folding nucleation-condensation is partially directed by formation of some secondary structure interactions. The correlation of the energy changes of mutants with inter-residue contact maps of the protein molecules provides a higher resolution than assigning the mutant data to certain positions in the polypeptide strand alone. In contrast to previous Phi-value analysis, we now can partially resolve folding motions. Compaction of at least one alpha-helix along its axis mediated by internal hydrogen bonds and stabilized by diffuse tertiary structure interactions appears to be one important molecular event during early folding in barstar, CI2, spectrin R16 domain, Arc repressor, alpha-lactalbumin, IM7, IM9, and spectrin R17 domain. A lateral movement of at least two strands neighbored in sequence towards each other appears to be involved in early folding of the SH3 domain, cspB, CTL9, and FKBP12.
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PMID:Protein folding forces. 1817 71