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The primary structure of 11s globulin subunit b in the seeds of cotton cultivar 108 f 4. high molecular weight peptides of the full tryptic hydrolysis and tryptic hydrolysis based on arginine residues of the subunit b






Khimiya Prirodnykh Soedinenii (2): 227-230

The primary structure of 11s globulin subunit b in the seeds of cotton cultivar 108 f 4. high molecular weight peptides of the full tryptic hydrolysis and tryptic hydrolysis based on arginine residues of the subunit b

Three high-MW peptides (Tp1,4,4; Tp1,3,3 and Tp1,1,2) were obtained from the full tryptic hydrolysate of the subunit B using paper chromatography and electrophoresis. These peptides constitute 165-170 amino acid residues of the polypeptide chain of the subunit. Peptide bonds of the basic amino acids stable to the effect of trypsin were present in the polypeptide chain of the subunit.


Accession: 006740818



Related references

Li, A.; Yunusov, T., 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. Chemistry of natural compounds 20(2): 209-212

Yunusov, T.S., 1984: The primary structure of 11s globulin subunit b in the seeds of cotton cultivar 108 f 3. peptides of the tryptic hydrolysis based on arginine residues. High-MW lysine-containing peptides were isolated from the tryptic hydrolysate of the subunit B based on arginine residues using gel chromatography. Their properties were described. These peptides are necessary for the reconstruction of the polypep...

Piyakina, G.A.; Yunusov, T.S.; Redina, E.F., 1984: The primary structure of 11s globulin subunit b in the seeds of cotton cultivar 108 f 2. peptides of the tryptic hydrolysis based on lysine residues. Six large lysine peptides were isolated from the tryptic hydrolysate of lysine subunit B using paper chromatography and electrophoresis. The peptides constitute 172 amino acid residues from the total 180-190 amino acid residues of the whole polype...

Yunusov, Ts, 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 characterize...

Piyakina, G.; Yunusov, T.; Redina, E., 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.

Li, A.; Yunusov, T.; Kal'-Metova, E., 1984: Primary structure of subunit B of the 11S globulin of seeds of cotton plant variety 108-F. I. Acid-souble peptides from complete tryptic hydrolysis of subunit B. Chemistry of natural compounds 20(1): 83-87

Anonymous, 1984: Primary structures of subunit of b of the 11s globulin of seeds of cotton plant variety 108 f 1 acid soluble peptides from complete tryptic hydrolysis of subunit b

Li, A.L.; Yunusov, T.S.; Kal'metova, E.R., 1984: Study of the primary structure of subunits in 11s globulin of cultivar 108 f cottonseeds 1. acid soluble peptides of complete tryptic hydrolysis of subunit b. Twenty low MW peptides were isolated from complete tryptic hydrolysate of subunit B. The amino acid sequence was determined for 13 peptides.

Lipkin, V.M.; Marchenko, T.V.; Khokhryakov, V.S.; Polovnikova, I.N.; Potapenko, N.A.; Modyanov, N.N.; Ovchinnikov-Yu, A., 1980: Primary structure of the beta subunit of escherichia coli dna dependent rna polymerase 2. low molecular weight peptides of limited tryptic hydrolysis. Ion-exchange chromatography on Aminex 50W .times. 4, gel filtration, paper chromatography and paper electrophoresis of the fractions IX and X (isolated by Sephadex G-100 chromatography from the products of the .beta.-subunit limited trypsinolysis)...

Anonymous, 1980: Primary structure of the beta subunit of escherichia coli dna dependent rna polymerase ec 2776 2 the low molecular weight peptides from limited tryptic hydrolysis