Results 281 to 290 of about 184,724 (334)
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Cyanogen bromide treatment of methionine-containing compounds
Biochemistry, 1977The preparation of a series of X-Met-Gly-OEt and X-Met-Phe-OMe and their treatment with CNBr in either 70% or 97-100% formic acid at 25 degrees C are described where X is methanesulfonyl (mesyl), p-nitrobenzyloxycarbonyl, phthaloyl, trifluoroacetyl, acetyl, formyl, or tert-butyloxycarbonyl.
Clement W. T. Yeung+2 more
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Biochemistry, 1977
The alpha chain of human fibrinogen consists of 600 +/- 25 amino acid residues, 10-11 of which are methionines. In this regard, we have identified and characterized 11 cyanogen bromide peptide fragments of 2, 3, 26, 28, 28, 37, 51, 56, 60 +/- 5, 64 +/- 5,
R. Doolittle+5 more
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The alpha chain of human fibrinogen consists of 600 +/- 25 amino acid residues, 10-11 of which are methionines. In this regard, we have identified and characterized 11 cyanogen bromide peptide fragments of 2, 3, 26, 28, 28, 37, 51, 56, 60 +/- 5, 64 +/- 5,
R. Doolittle+5 more
semanticscholar +1 more source
Biochemistry, 1975
Information compiled by automatic Edman degradation of Streptomyces griseus trypsin coupled with previous data has permitted the assignment of the first 36 residues at the NH2 terminus of the protein.
R. Olafson+3 more
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Information compiled by automatic Edman degradation of Streptomyces griseus trypsin coupled with previous data has permitted the assignment of the first 36 residues at the NH2 terminus of the protein.
R. Olafson+3 more
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Journal of the American Chemical Society, 2004
Herein cyanogen bromide is employed for the efficient production of N-terminal cysteine containing protein fragments for expressed protein ligation (EPL) from polyhistidine-tagged precursors.
D. Macmillan, Lubna Arham
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Herein cyanogen bromide is employed for the efficient production of N-terminal cysteine containing protein fragments for expressed protein ligation (EPL) from polyhistidine-tagged precursors.
D. Macmillan, Lubna Arham
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Cyanogen bromide splitting of human immunoglobulin M
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Human Waldenstrdm IgM (kappa) (Dau), its polypeptide chains and its F(c)5 micro and Fab micro fragments were split by cyanogen bromide (CNBr). The fragments formed by CNBr were fractionated by gel filtration, ion exchange chromatography and paper electrophoresis.
J. Claude Bennett, Jiří Zikán
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Template-directed polymerization of oligoadenylates using cyanogen bromide.
Biochemistry, 1986Cyanogen bromide (BrCN) condensed oligoadenylates [oligo(A)] on a poly(uridylic acid) [poly(U)] template in an aqueous solution. Imidazole and divalent metal ions such as Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Mg2+, and Fe2+ were required for the condensation ...
E. Kanaya, H. Yanagawa
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Cyanogen bromide fragments of human serum transferrin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Abstract Human serum transferrin was fragmented by a combination of methods involving cyanogen bromide, acylation, and reduction-alkylation. Six fragments were isolated in a homogeneous form, and their molecular weights were 26 000; 16 000; 15 000; 9000; 6000; and 4000 (the N-terminal fragment of transferrin), thus accounting for the molecular weight
Anatoly Bezkorovainy, Dietmar Grohlich
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Cyanogen Bromide Fragments of Rabbit Skeletal Tropomyosin
Canadian Journal of Biochemistry, 1973Previous studies have demonstrated that rabbit skeletal tropomyosin consists of two or more chemically non-identical but highly homologous polypeptide chains. Attempts by a variety of techniques to prepare pure tropomyosin chains in amounts adequate for chemical characterization have been unsuccessful to date. To provide more extensive information for
Lawrence B. Smillie, Robert S. Hodges
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[27] The cyanogen bromide reaction
1967Publisher Summary This chapter discusses the applications of the cyanogens bromide reaction. Cyanogen bromide is capable of cleaving thioethers. The action of cyanogen bromide upon proteins is unique in its selective attack on methionine. The reaction of methionine with cyanogen bromide is greatly facilitated by the strong neighboring group effect ...
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Pyridinoline fluorescence in cyanogen bromide peptides of collagen
Biochemical and Biophysical Research Communications, 1981Summary Pyridinoline is a fluorescent crosslinking amino acid of collagen fibers. But recently some investigators claimed that it is not a crosslink component but an artefact produced by the interaction of collagen and non-collagenous contaminants during acid hydrolysis.
Yohzoh Gotoh+2 more
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