Primary structure of subunit B of the 11S globulin of seeds of cotton plant variety 108-F. I. Acid-soluble peptides from complete tryptic hydrolysis of subunit B

The 11S globulin of cotton seeds consists of three types of subunits: A, B, and C. The complete tryptic hydrolysis of subunit B has given acid-soluble and acid-in-soluble peptides. The amino acid compositions and amino acid sequences of the acid-soluble peptides have been determined.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 88–93, January–February, 1984.     

Primary structure of subunit B of the 11S globulin of cotton seeds of variety 108-F. II. Peptides of tryptic hydrolysis at lysine residues

Six large lysine peptides have been isolated from a tryptic hydrolysate at lysine residues, making up all together 172 amino acid residues of the 180–190 amino acid residues of the whole polypeptide chain of the molecule.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 220–224, March–April, 1984.     

Primary structure of subunit B of the 11S globulin of cotton seeds of variety 108-F. III. Peptides from tryptic hydrolysis at arginine residues

To obtain peptides overlapping the lysine peptides obtained by complete tryptic hydrolysis, cleavage of maleylated subunit B with trypsin at arginine residues has been performed. Large peptides containing lysine have been obtained and characterized.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 224–227, March–April, 1984.     

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

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.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.     

The globulins of cotton seeds XIX. Chymotryptic and tryptic peptides of subunit C of the 11S globulin

Summary 1. The structures of 51 chymotryptic peptides isolated from a chymotryptic hydrolyzate of subunit C have been determined.2. The structures of 15 tryptic peptides from a tryptic hydrolyzate of subunit C have been established.3. On the basis of the structures of the peptides, the structure of the molecule of subunit C of the 11S globulin of cotton seeds has been established.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 613–621, September–October, 1978.     

A study of the globulins of the seeds of the cotton plant of variety 108-F and radiomutants

Chemistry of Natural Compounds -     

Dioxane lignin from shoots of the cotton plant of variety 108-F. I

The dioxane lignin has been isolated by Pepper's method from two-week shoots of the cotton plant of variety 108-F and has been separated into two fractions — insoluble and soluble in ether — DLA-A and DLA-B, respectively. It has been shown that in the early stage of development of the cotton plant a low-molecular-weight lignin with a low degree of methoxylation and distinctly different from the lignin from ripe stems of the same cotton plant is synthesized.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 96–98, January–February, 1984.     

Study of the total histone of the cotton plant of variety 108-F

From two-day etiolated shoots of the cotton plant of variety 108-F we have isolated the total histone and purified it on a column of CM-cellulose. It has been shown by gel electrophoresis and amino acid analysis that the total histone of the cotton plant, like the total histone of wheat, consists of five main fractions, the amount of the lysine-rich fraction A₁ being greater in the cotton plant than in wheat (23% and 19%, respectively), and the amount of arginine-rich fraction A₄ being less (19.2 and 24.3%, respectively). The total histone of the cotton plant is less basic (ratio of basic amino acids to acidic amino acids in the cotton-plant histone 1.24, in wheat histone 1.9, and in calf thymus histone 1.78) but richer in lysine as compared with arginine than the histones of wheat and calf thymus.V. I. Nikitin Institute of Chemistry, Academy of Sciences of the Tadzhik SSR, Dushanbe. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 109–112, January–February 1980.