Abstract
The high-molecular-weight peptides from the complete tryptic hydrolysis and tryptic hydrolysis at arginine residues of subunit B, which contained uncleaved bonds of the basic amino acids, have been studied. In the investigation of these peptides, use was made of additional cleavage by trypsin at lysine residues and of cyanogen bromide cleavage.
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A. L. Li, G. A. Piyakina, E. G. Yadgarov, T. Yu. Shadrina, S. I. Asatov, T. S. Yunusov, and P. Kh. Yuldashev, Khim. Prir. Soedin., 680 (1979).
W. R. Gray, Methods Enzymol.,25, 333 (1972).
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Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 227–230, March–April, 1984.
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Li, A.L., Yunusov, T.S. Primary structure of subunit B of the 11S globulin of cotton seeds of variety 108-F. IV. High-molecular-weight peptides from the complete tryptic hydrolysis and from tryptic hydrolysis at the arginine residues of subunit B. Chem Nat Compd 20, 209–212 (1984). https://doi.org/10.1007/BF00579485
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DOI: https://doi.org/10.1007/BF00579485