A study of the water-soluble proteins of the seeds of the cotton plants Gossypium hirsutum and G. barbadense

It has been shown by electrophoresis in polyacrylamide gel that different enzymes with similar electrophoretic mobilities may be localized in one and the same zone of water-soluble cottonseed proteins. Some zones not stained by the usual protein dyes also possess enzymatic activity. It has been established that the majority of the electrophoretic fractions consist of a series of polypeptides with different molecular weights, mainly of low-molecular-weight nature. The results are given of an investigation of the peroxidase, -amylase, lipase, NADH-DCPIP oxidoreductase, and NADPH-DCPIP oxidoreductase activities of the water soluble fraction of the proteins of the seeds of the species mentioned.Institute of Experimental Plant Biology, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 488–491, July–August, 1986.     

Comparative study of the physicochemical properties of the species-specific proteins of cotton plants of the speciesGossypium hirsutum andG. barbadense

Four species-specific proteins have been isolated for the first time: H.0.43 and H.0.51 from aG. hirsutum cotton plant, and B.0.37 and B.0.48 fromG. barbadense. The conditions are given for their separation on Sephadex G-100 and on DEAE-cellulose and for their preparative electrophoresis in PAAG. Their isoelectric points and molecular masses have been determined and their subunit compositions have been investigated.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 89 14 75. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 871–877, November-December, 1995. Original article submitted May 15, 1995.     

Comparative investigation of the molecular structures of the species-specific proteins of the seeds ofGossypium hirsutum andG. barbadense

The N-terminal amino acids and the amino acid compositions of four species-specific proteins of two species of the cotton plant —Gossypium hirsutum andG. barbadense — have been determined. Peptide maps of tryptic hydrolysates of these proteins have been obtained and compared. Individual tryptic peptides have been isolated and purified. The N-ends, amino acid compositions, and amino acid sequences of individual peptides have been determined. The N-terminal sections of the proteins ofG. hirsutum andG. barbadense as far as the 16th amino acid residue have been sequenced. A comparative analysis has been made of the peptides and proteins of these cottonplant species.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 40 64 75. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 858–864, November–December, 1997.     

Proteins of the seeds ofRicinis communis. I. A study of the water-soluble proteins of the seeds and meal ofRicinis communis

The electrophoretic spectrum of the water-soluble proteins of the seeds and meal of the castor-oil plant has been studied. A correlation has been found between a decrease in the relative amount of electrophoretic components with R_f 0.04 and 0.11 and the hemagglutinating activity of the meal.     

Interaction of abscisic-acid-binding cotton (Gossypium hirsutum) protein and phytohormones

The interaction of representatives of three classes of phytohormones, abscisic acid (ABA), the synthetic auxin 1-NAA, and the synthetic cytokinin 6-BAP, with ABA-binding cotton protein was studied. Binding of ABA with its protein was shown to be specific and receptor-like. Competitive protein binding showed that 1-NAA (15±3%), 6-BAP (82±3%), and ABA (95±3%) replace³H-ABA from the protein complex. The possibility of reacting ABA-binding protein with various classes of intracellular phytohormones is discussed.Institute of Genetics and Experimental Biology of Plants, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (99871) 64 22 30. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 252–253, May–June, 2000.     

Flavonol glycosides of the flowers of a thin-leaved cotton plant of the species Gossypium barbadense

Summary The flowers of the thin-leaved cotton plant of variety 5904-I(Gossypium barbadense) contained more than 5% of combined flavonols consisting of quercimeritrin, hisutrin, quercetin 3-glucoside, and a flavonol with mp 228–229°C. The latter has the structure of gossypetin 7--D-glucopyranoside.Scientific-Research Institute for the Chemistry and Technology of Cotton Cellulose, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 142–146, March, 1971.     

Proteins of the seeds ofRicinis communis. I. A study of the water-soluble proteins of the seeds and meal ofRicinis communis

The electrophoretic spectrum of the water-soluble proteins of the seeds and meal of the castor-oil plant has been studied. A correlation has been found between a decrease in the relative amount of electrophoretic components with R_f 0.04 and 0.11 and the hemagglutinating activity of the meal.Institute of the Chemistry of Plant Substances of the Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 630–631, September–October, 1960.     

Composition of the phospholipids of Gossypium barbadense

Summary 1. The combined phospholipids of the seed kernels of the cotton plant have been completely freed from accompanying carbohydrates by gel filtration on Molselekt G-25.2. It has been established by two-dimensional chromatography in a thin layer of silica gel that the phospholipids of the seed kernels of the cotton plant of thin-fibered variety 5904-I consist of X₁- and X₂-polygly cerophosphatides (2.4 and 7.1%, respectively), phosphatidylethanolamines (14.1%), phosphatidylcholines (50.4%), phosphatidylinositols (20.4%), and lysophosphatidylcholines (5.6%).3. The accompanying substances of the phospholipids of the cotton plant form two groups each of steroids and disaccharides.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 19–21, January–February, 1976.     

Enzyme peroxidase in calluses of cotton plants of the speciesGossypium hirsutum andG. herbaceum

A comparative study has been made of the activity of the enzyme peroxidase and its isozyme spectrum from two species of cotton plant. It has been found that, as calluses grow, new isoforms of peroxidase are produced and the protein content increases.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, fax 627071. Institute of Genetics, Academy of Sciences of the Republic of Uzbekistan, fax 642230. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 90–92, January–February, 1994.     

The chemical study of the main phospholipids of the seed kernels of cotton plants of the speciesGossypium barbadense

The qualitative and quantitative compositions and also the general and position distributions of the fatty acids of the seeds of the thin-fibered varieties of the cotton plant S-6022, S-6015, S-6034, S-6037, and 9123-I have been studied.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 291–294, May–June, 1984.