Advances in Protein Chemistry, Volume 21Advances in Protein Chemistry |
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Results 1-5 of 44
Page 8
... band in the ultraviolet (Am, 268.5 my) and ascribed this to the formation of a thiazoline ring (111) (compare 2 ... bands de— crease in intensity, whereas the C~N stretching bands increase (Martin and Edsall, 1958; Garfinkel, 1958). The ...
... band in the ultraviolet (Am, 268.5 my) and ascribed this to the formation of a thiazoline ring (111) (compare 2 ... bands de— crease in intensity, whereas the C~N stretching bands increase (Martin and Edsall, 1958; Garfinkel, 1958). The ...
Page 15
... band at 8.94 p. (corresponding to the band at 9.01 ,u. in CySOzSCy) and NATURALLY OCCURRING PEPTIDES 15.
... band at 8.94 p. (corresponding to the band at 9.01 ,u. in CySOzSCy) and NATURALLY OCCURRING PEPTIDES 15.
Page 16
(corresponding to the band at 9.01 ,u. in CySOzSCy) and solutions of the thiolsulfonate showed the expected property of reacting readily with thiols, e.g., cysteine, to give the mixed disulfide and the sulfinic acid: (}SO2SG + CySH ...
(corresponding to the band at 9.01 ,u. in CySOzSCy) and solutions of the thiolsulfonate showed the expected property of reacting readily with thiols, e.g., cysteine, to give the mixed disulfide and the sulfinic acid: (}SO2SG + CySH ...
Page 35
... bands at 5.93 M (COQH of glycine residue), 6.08 and 6.65 n (amide I and II bands), and 8.14n (C0; of glutamyl residue). The values for pKl, pKg, and pK3 were 2.39, 3.95, and 9.38, respectively (Calam and Waley, 1962). 4. Occurrence and ...
... bands at 5.93 M (COQH of glycine residue), 6.08 and 6.65 n (amide I and II bands), and 8.14n (C0; of glutamyl residue). The values for pKl, pKg, and pK3 were 2.39, 3.95, and 9.38, respectively (Calam and Waley, 1962). 4. Occurrence and ...
Page 48
... bands consistent with the presence of peptide bonds. The “lipophilic peptides” of the brain are somewhat similar, but here the amino acid composition is, to some extent, characteristic (Uzman, 1958; Uzman and Rosen, 1958; Uzman and ...
... bands consistent with the presence of peptide bonds. The “lipophilic peptides” of the brain are somewhat similar, but here the amino acid composition is, to some extent, characteristic (Uzman, 1958; Uzman and Rosen, 1958; Uzman and ...
Contents
Chapter 2 Cytochrome c | 113 |
Chapter 3 Hydrogen Exchange in Proteins | 287 |
Chapter 4 Selenium Derivatives in Proteins | 387 |
Author Index for Volume 21 | 417 |
Subject Index for Volume 21 | 438 |
Cumulative Author Index for Volumes 121 | 443 |
Cumulative Title Index for Volume 121 | 449 |
Common terms and phrases
Acta actinomycin activity amide amino acid aqueous solution baker’s yeast band Biochem Biol Biophys carnosine cells Chem chromatography chrome complex compounds concentration confirmed conformation containing cysteine cyto cytochrome oxidase deuterium disulfide enzymatic enzyme exchange rate exchanging hydrogen atoms extracts ferric ferricytochrome first fraction function glutamic acid glutathione glycine gramicidin groups GSSG H-D exchange heme heme peptide heme proteins hemochrome Hvidt hydrogen atoms hydrogen bonds hydrolysis hydrophobic imidazole infrared ionization iron isolated isotope effect Keilin kinetic exchange curves labile hydrogen atoms ligand Margoliash molecular muscle myoglobin native protein Nielsen observed obtained Okunuki ophthalmic acid oxidation Paléus peptide chain peptide-group hydrogen atoms Physiol polypeptide porphyrin preparations present primary structure Proc protein protein molecule purified rate constant reaction scheme redox residues ribonuclease Schwarz Section selenium selenium derivatives selenomethionine species specific studies sulfur synthesis temperature Theorell and Akesson thiol tion tissues titration Waley Yamanaka