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.     

Phosphono analogue of phosphatidylethanolamines from kenaf seeds

Institute of the Chemistry of Plant Substances, Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, Vol. 6, pp. 848–849, November–December, 1989.     

N-acylated phospholipids and lysophospholipids of kenaf seeds

Summary Three minor components have been isolated from the total PLs of kenaf seeds of variety Kuban'-333 by means of column and preparative thin-layer chromatography and they have been characterized by lysophosphatidylcholine and N-acylphosphatidylethanolamine and its lyso analog.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 723–725, November–December, 1976.     

Protein kinase from cotton seeds

A Ca²⁺-dependent protein kinase C, active at pH 6.5–8.0 has been found in cotton seeds for the first time. The localization of the enzyme in the seeds has been established and some of its properties are described (stability in various media, capacity for performing the phosphorylation of various substrates, activation by calcium ions). Highly active preparations of cottonseed protein kinase C have been isolated by biospecific chromatography.Institute of Bioorganic Chemistry, Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 255–259, March–April, 1989.     

Aspartate aminotransferase from cotton seeds

Chemistry of Natural Compounds - Using fractionation with ammonium sulfate and ion-exchange chromatography on CM- and DEAE-celluloses, two fractions with aspartate aminotransferase activity have...     

Aspartate aminotransferase from cotton seeds

Summary Using fractionation with ammonium sulfate and ion-exchange chromatography on CM- and DEAE-celluloses, two fractions with aspartate aminotransferase activity have been obtained from cotton seeds.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 735–738, November–December, 1970.     

Isolation of ribosomes from cotton seeds

Summary 1. It has been established that the method of precipitation with ethanol in the presence of an increased concentration of Mg²⁺ can be used for the rapid isolation of the ribosome fraction from plant material.2. The optimum conditions for the complete precipitation of the ribosome fraction from a homogenate of cotton seeds have been selected.3. By treating an extract of the seeds with 0.5 M KCl it was possible to reduce the amount of tRNA in a preparation of the total rRNA.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 852–856, November–December, 1977.     

Spectroscopic determination of the degree of esterification of pectic substances from kenaf

Pectins were isolated from bark, wood and pith of four kenaf (Hibiscus cannabinus L.) varieties. The degree of esterification of isolated pectins was studied using Fourier transform infrared spectroscopy. It was determined as being between 57 and 90% and there were no notable differences between kenaf varieties. The higher value of the degree of esterification was presented in wood pectins (86-90%), the interim in pith (75-83%) and the lower in bark (57-64%).     

Isolation of protease B from cotton seeds

Protease B has been isolated from dormant cotton seeds by fractionation with ammonium sulfate, ion-exchange chromatography on CM-cellulose, and gel filtration through Acrilex P-10 and Sephadex G-75, with 128-fold purification. The enzyme exists in dimeric and monomeric forms. According to the results of gel filtration, their molecular weights are 72,000 and 36,000, respectively. The enzyme consists of a single polypeptide chain including sugars. The N-terminal amino acid of protease B is alanine. The enzyme possesses proteolytic activity in the pH range from 4 to 6.     

Isolation of protease B from cotton seeds

Protease B has been isolated from dormant cotton seeds by fractionation with ammonium sulfate, ion-exchange chromatography on CM-cellulose, and gel filtration through Acrilex P-10 and Sephadex G-75, with 128-fold purification. The enzyme exists in dimeric and monomeric forms. According to the results of gel filtration, their molecular weights are 72,000 and 36,000, respectively. The enzyme consists of a single polypeptide chain including sugars. The N-terminal amino acid of protease B is alanine. The enzyme possesses proteolytic activity in the pH range from 4 to 6.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 506–510, July–August, 1984.     

Comparative study of the total tRNAs of the seeds of the cotton plant and the seeds ofGinkgo biloba

Summary 1. Three methionine tRNAs have been found both in the total tRNAs of cotton seeds and in those ofGinkgo biloba. In both cases only the first was acylated by methionine with the aid ofE. coli ARSases.2. Four phenylalanine tRNAs have been found in the total tRNAs of cotton seeds, and two in the tRNAs of ginkgo seeds.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 54–56, January–February, 1979.     

Isolation and characterization of protease inhibitors from cotton seeds

Protease inhibitors of protein nature have been isolated from dormant cotton seeds. The participation of protease inhibitors in the mechanism of protecting the plant from wilt damage is discussed.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. 3, pp. 445–448, May–June, 1995. Original article submitted June 27, 1994.