Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 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 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 primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown in Fig. 4. There are sequence homologies within protein L25 (Table 6) as well as between protein L25 and other ribosomal proteins (Table 5).
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PMID:The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes. 110 May 6

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 complete amino acid sequences of phospholipase A (Fractions DE-I and DE-II) from Naja melanoleuca (Forest cobra) have been elucidated. The reduced and S-carboxymethylated isoenzyme were digested with trypsin and thermolysin and the peptides were purified by ion-exchange chromatography, gel filtration and chromatography or electrophoresis on paper. The Edman procedure, either through the use of the automatic sequencer or by manual manipulation, was employed to obtain the sequences of the intact isoenzymes and the pure peptidesmthe thermolysin digest provided the necessary overlapping peptides which allowed the alignment of the tryptic peptides of Fraction DE-I. The tryptic peptides of Fraction DE-II were either identical or homologous to the tryptic peptides of Fraction I and Fraction III [12] and were aligned in the same order as that of Fractions DE-I or DE-III. The amino acid sequence of N. melanoleuca phospholipase A, Fraction I, shows a high degree of homology with Fraction DE-II and also with Fraction DE-III, previously reported on [12].
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PMID:The amino acid sequence of phospholipase A, fractions DE-I and DE-II. 112 92

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

The structure of the major human erythrocyte membrane protein (protein E) was investigated by studying the products of proteolysis of the native protein in the membrane. The distribution and location of the tyrosine residues labelled by radioiodination by lactoperoxidase was determined. Proteolysis of the extracellular region of the protein by thermolysin released four tyrosine-containing peptides, all of which were also found to remain in the major fragment that is retained in the membrane. The presence of these duplicated sites in the extracellular region of the protein was confirmed by limited trypsin digestion of the intracellular region of the protein. Two groups of fragments were obtained. Both groups contained a set of the extracellular labelled sites, but they differed in containing distinct groups of intracellular sites, showing that the two sets of extracellular sites are linked by an intracellular region of the protein. The polypeptide chain thus traverses the membrane twice. An S-shaped model which is consistent with these data is proposed.
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PMID:The major human erythrocyte membrane protein. Evidence for an S-shaped structure which traverses the membrane twice and contains a duplicated set of sites. 116 51

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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