Disulphide bonds in wheat gluten: isolation of a cystine peptide from glutenin
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Keywords:
Glutenin
Thermolysin
Edman degradation
Sephadex
Gel permeation chromatography
Protein primary structure
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.
Thermolysin
Edman degradation
Protein primary structure
Pepsin
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Citations (12)
Isolated cyanogen bromide fragments of the αB 2 chain of α‐crystallin contained 67 and 107 residues, respectively. Part of the sequence of the C‐terminal fragment was elucidated by Edman and Begg sequenator analysis. Sequences of the tryptic peptides were determined by a combination of various Edman degradation techniques. Overlaps of tryptic peptides were established by selective modification of lysine residues and subsequent tryptic cleavage and by isolation of peptides after hydrolysis with chymotrypsin, thermolysin and a staphylococcal protease. The sequence of the αB 2 chain comprises 175 residues corresponding to a molecular weight of 20070. This value is somewhat lower than that assumed hitherto. A high degree of homology between the αB 2 , and the αA 2 chain, the major polypeptides, of bovine α‐crystallin was observed.
Cyanogen bromide
Edman degradation
Thermolysin
Protein primary structure
Cleavage (geology)
Homology
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Citations (182)
Paim I, a protein alpha-amylase inhibitor, inhibits animal alpha-amylases from pig, dog, cow, horse, etc. but has no activity against human salivary and pancreatic amylases. The primary structure of Paim I has been determined by Edman degradation and fast atom bombardment mass spectrometry (FABMS). This protein is a single-chain polypeptide of 73 amino acid residues with a calculated molecular weight from the sequence data of 7415.3 (monoisotopic molecular weight) and 7420.2 (average molecular weight). The sequencing strategy chosen for Paim I consists of four steps. First, the accurate molecular weights of the intact and tetra-S-carboxymethylated Paim I are determined by fast atom bombardment mass spectrometry. Second, the primary fragments generated by Staphylococcus aureus V8 protease are isolated by reversed-phase high-performance liquid chromatography. The molecular weights of these subpeptides are determined by FABMS. The peptides that must be sequenced are selected by the molecular weights of these subpeptides and the tetra-S-carboxymethylated Paim I. Third, these subpeptides and the whole protein are sequenced by automated Edman degradation. Finally, the primary structure of tetra-S-carboxymethylated Paim I is confirmed by the combination of tryptic, chymotryptic, and S. aureus V8 protease digestion and FABMS. The sequence of Paim I is compared with those of Haim II, Hoe-467A, Z-2685, and AI-3688 because they have different alpha-amylase inhibition spectra against mammalian alpha-amylases but belong to a family of related proteins.
Edman degradation
Fast atom bombardment
Protein primary structure
Molecular mass
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Citations (32)
The complete primary structure of turkey muscle acylphosphatase has been determined. The sequence was derived from peptides obtained by digestion of the carboxymethylated protein with pepsin and thermolysin and by subdigestion of some of the cyanogen bromide fragments with trypsin and Staphylococcus aureus protease. Peptides were purified by preparative finger prints and/or preparative high-performance liquid chromatography. Sequencing of the various peptides was achieved by manual Edman degradation and by time-course analysis of amino acids released by carboxypeptidases. The amino-terminal blocking group (acetyl) was determined by fast atom bombardment mass spectrometry. This sequence was compared with that of horse muscle enzyme determined previously.
Thermolysin
Edman degradation
Cyanogen bromide
Protein primary structure
Pepsin
Fast atom bombardment
Digestion
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Citations (22)
Journal Article Amino Acid Sequence of Immunity Protein (B Subunit) of ColicinE3 Get access Katsumi MOCHITATE, Katsumi MOCHITATE Department of Biochemistry, Faculty of Medicine, The University of TokyoHongo, Bunkyo-ku, Tokyo 113 Search for other works by this author on: Oxford Academic PubMed Google Scholar Koichi SUZUKI, Koichi SUZUKI Department of Biochemistry, Faculty of Medicine, The University of TokyoHongo, Bunkyo-ku, Tokyo 113 Search for other works by this author on: Oxford Academic PubMed Google Scholar Kazutomo IMAHORI Kazutomo IMAHORI Department of Biochemistry, Faculty of Medicine, The University of TokyoHongo, Bunkyo-ku, Tokyo 113 Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 89, Issue 5, April 1981, Pages 1609–1618, https://doi.org/10.1093/oxfordjournals.jbchem.a133356 Published: 01 April 1981 Article history Received: 17 November 1980 Published: 01 April 1981
Thermolysin
Edman degradation
Protein primary structure
Protein sequencing
Sequence (biology)
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Citations (18)
Thermolysin
Edman degradation
Protein primary structure
Ion chromatography
Cyanogen bromide
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Citations (28)
The primary structure of the 28‐peptide thymosin α 1 as determined by Goldstein et al. (1) has been confirmed by independent procedures. Limited dilute acid digestion generated a 26‐peptide and a 22‐peptide both extending to the C‐terminal and lacking the N‐terminal blocking group. A combination of Edman microsequencing, carboxypeptidase Y and thermolysin digestion, and fast atom bombardment mass spectrometry was used.
Primary (astronomy)
Thymosin
Enzymatic Hydrolysis
Protein primary structure
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Citations (7)
The amino acid sequence of component C 1 , the polypeptide specific for subunit F of prostatic binding protein, the major secretory glycoprotein of the rat ventral prostate, has been determined. Its structure was established using the manual Edman degradation on the intact protein and on the most relevant fragments isolated from trypsin, chymotrypsin, thermolysin and Staphylococcus aureus protease digests of the 14 C‐labelled S‐carboxamidornethylated component C 1 . Component C 1 contains 88 amino acids corresponding to a molecular weight of 10246. It is an acidic polypeptide due to the presence of 17 acidic residues; its thrce cysteine residues are almost symmetrically distributed over the peptide chain. Highly polar regions are found in positions 17‐27 and 37‐47, while the C‐terminal part of the molecule contains two hydrophobic segments
Thermolysin
Edman degradation
Protein primary structure
Cyanogen bromide
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Citations (19)
Edman degradation
Thermolysin
Protein primary structure
Cyanogen bromide
Ribosomal protein
Proteolysis
Protein sequencing
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Citations (20)
Thermolysin
Edman degradation
Protein primary structure
Residue (chemistry)
Glutamic acid
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Citations (9)