An investigation of cottonseed globulins. XXI. The 11S globulins of two varieties of the cotton plant

The 11S globulins of two varieties of the cotton plant — 108-F and Tashkent-1 — have been studied. It has been shown that the 11S globulins do not differ in quaternary structure and each consists of three subunits A, B, and C. It has been found that the subunits of these varieties differ in their amino acid compositions and the peptide maps of tryptic and chymotryptic hydrolysates.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 680–684, September–October, 1979.     

A study of the globulins of cotton seeds in the growth process

Summary 1. The 11S and 7S globulins of cotton seeds break down in the first five days of the growth of the seeds.2. During growth, the proteins dissociate into low-molecular-weight polypeptide chains without the formation of intermediate subunits.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 633–636, September–October, 1976.     

Denaturation and renaturation of the 11S globulin of cotton seeds by polarography

It has been established by a polarographic analysis of the globulins of cotton seeds that the 7S and 11S golublins possess a two-step polarographic wave with a half-wave potential of –1.42 V. On the basis of the results of a study of the kinetics of thermal denaturation the high lability of the 11S globulin on heating has been shown. The conditions have been determined of the complete denaturation of the 11S globulin in 8 M urea solution and it has been established that the latter is an irreversible process.Institute of the Chemistry of Plant Substances of the Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 809–813, November–December, 1980.     

Physicochemical properties and substrate specificity of protease C from dormant cotton seeds

The substrate specificity of a proteolytic enzyme — protease C — isolated from cotton seeds has been studied. The activity of protease C is suppressed completely under the action of diisopropyl phosphorofluoridate. Protein inhibitors — duck ovomucoid, soybean inhibitor, and also TPCK — suppressed the activity of protease C to different degrees. On the basis of results obtained in the hydrolysis of the cottonseed reserve proteins, 7S and 11S globulins, and the B chain of insulin, protease C has been assigned to the serine group of endopeptidases. The optimum conditions — pH, time, and temperature — at which protease C exhibits its maximum activity has been determined.Institute of Chemistry of Plant Substances, Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 744–746, September–October, 1988.     

Conformational changes in the reserve proteins of the cotton plant

A quantitative study of the secondary structures of the 11S and 7S globulins from cotton seeds has been made by the circular dichroism (CD) method. It has been established that the 11S and 7S globulins contain, respectively: 16 and 14% of -helices; 15% each of -structures; 18 and 20% of -bends; and 51% each of irregular sections.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 355–357, May–June, 1984.     

The globulins of cotton seeds XI. The structure of the chymotryptic peptides of the 7S globulin

Summary The amino-acid sequences of the chymotryptic peptides of the 7S globulin of cotton seeds have been determined.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 682–687, September–October, 1977.     

Detection and synthesis of a synergist of the sex pheromone of the cotton bollworm

The synergisic properties of docosa-5Z, 17Z-diene — one of the by-products of the synthesis of the synthetic cotton bollworm pheromone — have been revealed.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 130–132, January–February, 1994.     

Polar lipids of cotton seeds and the products of their processing

The compositions and amounts of polar lipids in cotton seeds and the products of their processing have been investigated. Six glycolipids have been identified, the main ones being monogalactosyldiglyceride (MGDGs), digalactosyldiglycerides (DGDGs), and sterol glycosides. The fatty acid compositions of the neutral lipids and of the phospho- and glycolipids have been determined. In the glycolipids, saturated fatty acids — palmitic and stearic — predominated.Institute of Chemistry of Plant Substances, Uzbekistan Republic Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 194–198, March–April, 1993.     

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.     

Effect of the irradiation of cotton seeds with pulses of concentrated light on the composition of the cottonseed oil

The presowing irradiation of cotton seeds with pulses of concentrated light (PCL) causes a change in a number of indices of the oil. When the seeds are stored, oxidative processes in them are intensified. In the oil of the harvested seeds some indices are restored.Institute of the Chemistry of Plant Substances of the Academy of Sciences of the Uzbek SSR, Tashkent, and S. V. Starodubtsev Institute of Technical Physics of the Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 777–780, November–December, 1980.     

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.     

The globulins of cotton seeds X. Structures of tryptic peptides of the 7S globulin

Summary The amino-acid sequences of the tryptic peptides of the 7S globulin of cotton seeds have been determined.An analysis of the peptides obtained has been performed and on the basis of the overlapping chymotryptic peptides the sequence of tryptic peptides in the chain of the 7S globulin 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. 679–682, September–October, 1977.     

Isolation of the cytoplasmatic 5S ribosomal RNA from cotton seeds by preparative electrophoresis

Summary 1. The complete separation of low-molecular-weight 5S rRNA and tRNA from fractions of high-molecular-weight rRNAs (28S + 18S) in a preparation of the total rRNA from cotton seeds has been achieved.2. The optimum conditions have been selected for the preparative electrophoresis and isolation of homogeneous preparations of 5S rRNA and total tRNA.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 489–494, July–August, 1978.     

Isolation of proteins from cottonseed meal II. The salt method

Summary On the basis of the results of a study of the amino acid compositions of various protein fractions from cottonseed flour and meal it has been established that the fraction of salt-soluble proteins (globulins) does not change its composition and properties in the processing of cotton seeds. The yield of protein from the industrial meal using the salt-extraction method is 16%.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 626–628, September–October, 1974.     

Synthesis of hexadec-9Z-enal — One of the components of the sex pheromone of Heliothis armigera

Hexadec-9Z-enal — a component of the sex pheromone of the cotton bollwormHeliothis armigera — has been obtained by a three-stage synthesis from 9-acetoxynonanal and n-heptyltriphenylphosphonium bromide followed by reduction and oxidation.A. S. Sadykov Institute of Bioorganic Chemistry, Uzbekistan Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 276–277, March–April, 1992.     

Kinetics of the level of lipids in a cotton plant of variety 6524 S during maturation

The composition and amount of lipids in the seeds and leaves of the cotton plant of variety 6524 S over the vegetation periods have been investigated. The rate of biosynthesis of neutral lipids in cotton seeds in the 20-day period after flowering to the moment of maturation increases by a factor of 1.6 while the amounts of phospho- and glycolipids decrease by factors of 3.9 and 4.3, respectively. The fatty acid compositions of the neutral lipids and of the phospho- and glycolipids of the seeds and leaves have been determined.Institute of Chemistry of Plant Substances, Academy of Sciences of the Uzbekistan Republic, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 359–362, May–June, 1993.     

A study of the 11S globulin from cotton seeds IX. Structure of the glycopeptide

Summary 1. The oligosaccharide of the glycopeptide (I) from subunit C of the 11S globulin of cotton seeds consists of one molecule of glucosamine and three molecules of mannose.2. The oligosaccharide is attached to the protein through the glucosamine and has a branched structure.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 675–678, September–October, 1977.     

Protease A from cotton seeds. Isolation and purification of the enzyme

Protease A has been isolated in the homogeneous state from dormant seeds of cotton plants of the Tashkent-I variety. A scheme is proposed for the isolation and purification of the enzyme which includes the following stages: extraction of the defatted seeds with 0.1 M phosphate buffer, pH 7.4; precipitation of the protein with ammonium sulfate at 60% saturation; desalting by dialysis; and ionexchange chromatography on a column containing CM- and DEAE-celluloses. The molecular weight of the enzyme has been determined as 60,000. The enzyme efficiently hydrolyzes azocasein and the 7S and 11S reserve proteins of cotton seeds. Its maximum activity appears at pH 6.4–7.4 and a temperature of 35–40°C; it is not activated by sulfhydryl reagents and loses its activity in the presence of diisopropyl phosphorofluoridate. The assumption is made that protease A belongs to the serine type of trypsin-like proteases.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 738–741, November–December, 1986.     

Lipolytic enzymes of cotton seeds V. Triacetinase

Summary A triacetinase has been isolated from cotton seeds by the methods of gel filtration and ion-exchange chromatography. The homogeneity of the enzyme was shown by rechromatography, electrophoresis, ultracentrifugation, and a determination of the terminal amino acid. The molecular weight of the triacetinase obtained by four different methods (column gel filtration, thin-layer chromatography, ultracentrifugation, and amino-acid composition) is 18,000±1200. The amino-acid composition and the N-terminal amino-acid residue — methionine — have determined.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 767–770, November–December, 1974.     

Isolation of the total tRNA from cotton seeds

Summary 1. A comparative study has been made of various methods of isolating the tRNA from cotton seeds. It has been found that the best results are given by extraction of cotton seeds with a mixture of 80% phenol and 0.14 M NaCl.2. The conditions have been worked out for the preparative isolation of the total tRNA.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 621–624, September–October, 1978.