Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 complete amino-acid sequence of rabbit skeletal troponin-T is reported. The protein consists of a single polypeptide chain of 259 amino acids; it has an acetylated amino terminus and a molecular weight of 30,503. The sequence was determined by manual and/or automated Edman degradation techniques on the six fragments obtained after cleavage with cyanogen bromide. The larger fragments were further digested with trypsin, chymotrypsin, alpha-lytic protease, thermolysin, or pepsin to obtain smaller fragments suitable for manual sequencing. About 50% of the residues are charged at neutral pH with highly acidic amino-terminal (residues 1-39) and highly basic carboxyl-terminal regions (residues 221-259). Predictions of secondary structure indicate 37% helical content with two long sections (residues 80-102 and 122-146) in that portion of the molecule implicated in binding to tropomyocin. Two of the three phosphorylated sites in the molecule are located at serine-1 and serine-149 or -150. The sequence about the latter site resembles somewhat the phosphorylase kinase phosphorylation sites in phosphorylase alpha and troponin-I.
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PMID:Amino-acid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin. 106 62

The amino acid sequences of two cyanogen bromide fragments from porcine pepsin have been determined. Fragment CB3 which represents the NH2-terminal 80 residues of pepsin was assembled from the peptides purified from proteolytic digests of this fragment using alpha-chymotrypsin, thermolysin, and staphylococcal protease. Two chymotryptic peptides were isolated from the NH2-terminal region of this fragment. One of these contains 2 extra residues, Ala-Leu-, at the NH2 terminus. This peptide is apparently derived from a different cleavage site of pepsinogen in its conversion to pepsin. The second cyanogen bromide fragment, CB4, contains 47 residues. The sequence was established from the peptides resulting from proteolytic digests using alpha-chymotrypsin, alpha-lytic protease, and thermolysin. An isoleucyl residue at position 29 of fragment CB4 appears to be absent in some molecules. This represents a structural variant of pepsin.
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PMID:Primary structure of porcine pepsin. II. Amino acid sequence of two cyanogen bromide fragments, CB3 and CB4. 109 37

The complete amino acid sequence of mohair protein, SCMKB-M1.2 (97 residues), was determined. The protein was isolated from reduced and carboxymethylated mohair by chromatography on DEAE-cellulose phosphate. Peptides for sequence determination were obtained by digestion with trypsin, pepsin, chymotrypsin, thermolysin and papain, and were fractionated by DEAE-cellulose chromatography, paper chromatography and electrophoresis. The sequence of the peptides were determined by the Edman degradation method (by use of both the Beckman Sequence and a non-automatic procedure), and by partial acid hydrolysis. The protein is closely homologous to wool protein SCMKB-IIIB2, and also contains acetylated alanine as N-terminal amino acid.
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PMID:Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2. 109 56

After digestion of protein S4 with trypsin, all 32 tryptic peptides were isolated. Their amino acid compositions were analyzed and the sequence of the amino acids within the tryptic peptides was determined by means of a solid-phase peptide sequenator and by exopeptidases. Alignment of the tryptic peptides was established by analyzing and partially sequencing peptides isolated after digestion of the S4 protein with chymotrypsin, thermolysin and a glutamic-acid-specific protease. Further information about the alignment of peptides came from treatment of S4 with CNBr and with a lysine-modifying reagent.
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PMID:Determination of the complete amino-acid sequence of protein S4 from Escherichia coli ribosomes. 110 Mar 94

The lac repressor from Escherichia coli, composed of four identical subunits with a molecular weight of 37160, was carboxymethylated and fragmented by tryptic digestion and cyanogen bromide treatment. Using ion-exchange chromatography, gel filtration and preparative thin-layer electrophoresis and chromatography 29 of the 30 tryptic peptides were isolated in pure form. Direct Edman degradation and the dansyl-Edman technique were used to determine the sequence of the small tryptic peptides. Special emphasis was put on the sequence determination of the six large tryptic fragments which together account for 177 residues, corresponding to 51% of the repressor subunit with its 347 residues. The large tryptic fragments were analyzed after fragmentation with chymotrypsin, thermolysin and dipeptidyl aminopeptidase I. Thus the sequence of all 30 tryptic peptides could be deduced. The complete sequences of all cyanogen bromide fragments were deduced from peptides obtained by tryptic, chymotryptic and thermolytic digestion of the individual fragments and by automated stepwise Edman degradation of lac repressor and of the large cyanogen bromide fragments. The order of the cyanogen bromide fragments was given by overlapping tryptic peptides. The resulting amino acid composition of the monomer is Asp15, Asn11, Thr18, Ser30, Glu14, Gln27, Pro13, Gly22, Ala44, Cys3, Val33, Met9, Ile17, Leu40, Tyr8, Phe4, Trp2, Lys11, His7, Arg19. The sequence of lac repressor shows no similarities with that of other proteins known to bind to DNA or RNA. The N-terminal 55 residues contain two homologous regions. This part of the sequence which is involved in lac operator binding might have been formed by gene duplication.
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PMID:Amino-acid sequence of lac repressor from Escherichia coli. Isolation, sequence analysis and sequence assembly of tryptic peptides and cyanogen-bromide fragments. 110 32

Reduced and S-carboxymethylated phospholipase A (Fraction DE-III) from Naja melanoleuca venom was digested with trypsin, chymotrypsin and thermolysin. The resulting peptides were purified by ion-exchange chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 or G-50 and chromatography and electrophoresis on paper. The amino acid sequences of the intact enzyme and the pur peptides were determined by the Edman procedure, either through the use of the automatic sequencer or by manual manipulation. The chymotryptic digest provided the necessary overlapping peptides which allowed the alignment of the tryptic peptides into a single chain of 119 amino acids. The amino acid sequence of N. melanoleuca phospholipase A shows a high degree of homology with phospholipases A from Bitis gabonica and also from porcine pancreas.
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PMID:Naja melanoleuca (forest cobra) venom. The amino acid sequence of phospholipase A, fraction DE-III. 112 91

The amino acid sequences of three fragments obtained on cyanogen bromide cleavage of human transferrin have been determined. Two of the fragments are small (4 and 7 residues) and had not been isolated in previous studies of the CNBr fragments of transferrin. The sequence of the larger fragment (53 residues) was elucidated by examining peptides isolated from digests of the fragment with trypsin, chymotrypsin or thermolysin. This region of transferrin appears to contain the sites of three previously-reported substitutions in the D1 and D-chi genetic variants.
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PMID:The amino-acid sequences of three cystine-free cyanogen-bromide fragments of human serum transferrin. 112 16

1. RNAase (ribonuclease) U2, a purine-specific RNAase, was reduced, aminoethylated and hydrolysed with trypsin, chymotrypsin and thermolysin. On the basis of the analyses of the resulting peptides, the complete amino acid sequence of RNAase U2 was determined, 2. When the sequence was compared with the amino acid sequence of RNAase T1 (EC 3.1.4.8), the following regions were found to be similar in the two enzymes; Tyr-Pro-His-Gln-Tyr (38-42) in RNAase U2 and Tyr-Pro-His-Lys-Tyr (38-42) in RNAase T1, Glu-Phe-Pro-Leu-Val (61-65) in RNAase U2 and Glu-Trp-Pro-Ile-Leu (58-62) in RNAase T1, Asp-Arg-Val-Ile-Tyr-Gln (83-88) in RNAase U2 and Asp-Arg-Val-Phe-Asn (76-81) in RNAase T1 and Val-Thr-His-Thr-Gly-Ala (98-103) in RNAase U2 and Ile-Thr-His-Thr-Gly-Ala (90-95) in RNAase T1. All of the amino acid residues, histidine-40, glutamate-58, arginine-77 and histidine-92, which were found to play a crucial role in the biological activity of RNAase T1, were included in the regions cited here. 3. Detailed evidence for the amino acid sequence of the sequence of the proteins has been deposited as Supplementary Publication SUP 50041 (33 PAGES) AT THE British Library (Lending Division)(formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.
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PMID:The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena. 115 64

Primary structural studies have been carried out on the light chain of a homogeneous rabbit antibody to Group C streptococcal carbohydrate. Approximately 20 g of this antibody were obtained by multiple exchange transfusions at the peak of the antibody response. The isolated antibody was homogeneous by several antigenic and chemical criteria. The light chain was isolated and modified, and then digested with alpha-chymotrypsin or thermolysin. The resulting peptides were isolated by gel filtration, paper electrophoresis, and paper chromatography. The amino acid sequences of these peptides were determined by Edman degradation plus dansylation. This supplied sufficient information to assign approximately 90 percent of the residues in the chain. The destruction of tyrosine during acid hydrolysis of peptides which had been eluted from a paper chromatogram was investigated. This destruction is due to inpurities in the paper which contaminate the peptides. Prevention of such destruction can be achieved by predevelopment of the paper with 1 N NH4OH prior to paper chromatography.
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PMID:Primary structure of the L chain from a rabbit homogeneous antibody to streptococcal carbohydrate. I. Purification of antibody and sequence determination of peptides from alpha-chymo-tryptic and thermolytic digests. 116 92

After enzymatic digestion of chicken myoglobin by trypsin, chymotrypsin or thermolysin, the separation of peptides was performed by column chromatography on various ion exchange resins. Each peptide was purified by high-voltage paper electrophoresis or by chromatography either on paper or on ion-exchange resin, and its complete amino acid sequence was then determined by the combined dansyl-Edman procedure and by endopeptidase digestions. The whole globin was submitted to automatic Edman degradation using the Beckman sequencer. Residues have been positioned from overlaps of sequence data between tryptic (T), chymotryptic (C) and thermolysin (Th) peptides. The stepwise degradation of the whole globin confirmed the alignment of the N-terminal third of the molecule. The combination of these different approaches has led to the complete determination of the 153 residues sequence forming the polypeptide chain of chicken myoglobin. Comparison of the established chicken myoglobin structure with those from other species shows a conservation of structure, although the avian protein exhibits more variations in its amino acid sequence than has been found between other known myoglobins which all belong to mammalian species.
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PMID:The primary sequence of chicken myoglobin (Gallus gallus). 116 72


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