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The disulphide bonds of insulin.
Biochem J. 1955 Aug;60(4):541-56
PMID: 13249947
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The N-terminal and C-terminal amino acid sequence of calf rennin.
Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):147-51
PMID: 4399042
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The thiol sequences and sub-units of light meromyosin fraction 1.
Biochem J. 1967 Sep;104(3):44P
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Structure and evolution of immunoglobulins.
Prog Biophys Mol Biol. 1970;21:209-63
PMID: 4194548
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The effects of complete modification of amino groups on the antibody activity of antihapten antibodies. Reversible inactivation with maleic anhydride.
Biochemistry. 1968 May;7(5):1941-50
PMID: 5689844
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Thin-layer chromatography of 1-dimethylaminonaphthalene-5-sulphonyl derivatives of amino acids present in superfusates of cat cerebral cortex.
Biochem J. 1967 Apr;103(1):79-85
PMID: 6033776
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Reversible blocking of amino groups with citraconic anhydride.
Biochem J. 1968 Sep;109(2):312-4
PMID: 5679376
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The determination of the order of lysine-containing tryptic peptides of proteins by diagonal paper electrophoresis. A carboxyl-terminal sequence for pepsin.
Eur J Biochem. 1967 Jul;2(1):84-9
PMID: 4866857
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The primary structure of porcine pancreatic elastase. The N-terminus and disulphide bridges.
Biochem J. 1967 May;103(2):497-507
PMID: 5340368
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Three-dimensional Fourier synthesis of tosyl-elastase at 3.5 å resolution.
Nature. 1970 Feb 28;225(5235):806-11
PMID: 5415109
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The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains.
Biochem J. 1969 May;112(5):679-89
PMID: 5821728
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Direct evidence for the presence of histidine in the active center of chymotrypsin.
Biochemistry. 1963 Mar-Apr;2:252-5
PMID: 13992248
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Inter heavy-light chain disulphide bridge in immune globulins.
Nature. 1967 Apr 1;214(5083):92-4
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A diagonal paper-electrophoretic technique for studying amino acid sequences around the cysteine and cystine residues of proteins.
Biochem J. 1967 Dec;105(3):1203-7
PMID: 16742547
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ALKYLATION OF THE METHIONINE RESIDUES OF RIBONUCLEASE IN 8 M UREA.
J Biol Chem. 1964 Nov;239:3755-61
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The disulphide bridges and soluble tryptic peptides of calf rennin.
Biochem J. 1967 Sep;104(3):1064-74
PMID: 4860634
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Evolutionary similarities between pancreatic proteolytic enzymes.
Nature. 1965 Sep 11;207(5002):1157-9
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Tryptic cleavage at cysteinyl peptide bonds.
Biochem Biophys Res Commun. 1963 Mar 25;10:467-72
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The active centre of chymotrypsin. I. Labelling with a fluorescent dye.
Biochim Biophys Acta. 1956 Jul;21(1):58-70
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Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.
Biochem J. 1966 Oct;101(1):214-28
PMID: 5971783
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The disulfide bonds of ribonuclease.
J Biol Chem. 1960 Mar;235:648-59
PMID: 13833122
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Histidine sequences in the active centres of some 'serine' proteinases.
Biochem J. 1966 Oct;101(1):232-41
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Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen.
Nature. 1968 Apr 27;218(5139):343-6
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Separation of dansyl-amino acids by polyamide layer chromatography.
Biochim Biophys Acta. 1967 Feb 21;133(2):369-70
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THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551.
Biochem J. 1963 Nov;89:379-80
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Acidic peptides of the lens. 8. S-(alpha beta-dicarboxyethyl) glutathione.
Biochem J. 1963 Feb;86:226-31
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Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.
Nature. 1966 Aug 6;211(5049):591-3
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AMINO-ACID SEQUENCE OF BOVINE CHYMOTRYPSINOGEN-A.
Nature. 1964 Mar 28;201:1284-7
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The disulphide bridges of bovine chymotrypsinogen B.
Biochem J. 1967 Dec;105(3):1125-33
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II. Acid proteinases. Chemical studies of porcine pepsin.
Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):125-33
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Molecular structural effects produced in proteins by reaction with succinic anhydride.
Biochim Biophys Acta. 1958 Sep;29(3):587-93
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Three-dimensional structure of tosyl-alpha-chymotrypsin.
Nature. 1967 May 13;214(5089):652-6
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Reactions of N-ethylmaleimide with peptides and amino acids.
Biochem J. 1964 Jun;91(3):589-95
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An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
Biochem J. 1969 Jun;113(2):377-86
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Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease.
J Biol Chem. 1962 Jun;237:1856-60
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Pepsin from pepsinogen. Preparation and properties.
J Biol Chem. 1966 Nov 10;241(21):4940-50
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Disulphide interchange reactions.
Biochem J. 1955 Aug;60(4):535-40
PMID: 13249946
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Amino acid sequence of C-terminal fragment of hog pepsin.
Eur J Biochem. 1970 Apr;13(3):447-54
PMID: 4910388
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INTRAMOLECULAR MODELS DEPICTING THE KINETIC IMPORTANCE OF "FIT" IN ENZYMATIC CATALYSIS.
Proc Natl Acad Sci U S A. 1960 Apr;46(4):402-4
PMID: 16590620
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Studies on the disulfide bridges in ribonuclease.
Biochim Biophys Acta. 1957 Jun;24(3):633-5
PMID: 13436490
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Selective purification of the thiol peptides of myosin.
Biochem J. 1968 Apr;107(4):531-48
PMID: 5660634
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A diagonal electrophoretic method for selective purification of methionine peptides.
Biochem J. 1967 Feb;102(2):593-9
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Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin.
Biochem J. 1952 May;51(2):155-67
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Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases.
Nature. 1970 Feb 28;225(5235):802-6
PMID: 5415108
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Amino acid sequences around the disulphide bridges and methionine residues of porcine pepsin.
Biochem J. 1970 Jul;118(4):611-23
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Sub-unit structure and specificity of methionyl-transfer-ribonucleic acid synthetase from Escherichia coli.
Biochem J. 1968 Jun;108(2):281-8
PMID: 4874971