Primary structure of triacetinase — An esterase from cotton seeds IV. Peptides of the chymotryptic and thermolytic hydrolysis of cyanogen bromide fragments of triacetinase

Summary 1. Peptides from a chymotryptic hydrolyzate of cyanogen bromide fragment B-7 have been isolated and characterized. The structure of some peptides of the chymotryptic hydrolyzate have been studied and this has enabled the tryptic peptides to be linked up.2. The peptides of a thermolysin hydrolyzate of cyanogen bromide B-5 have been isolated and characterized. The study of the structure of the thermolysin peptides has permitted the linking of two tryptic peptides.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 248–253, March–April, 1978.     

Primary structure of triacetinase — An esterase from cotton seeds III. Peptides from tryptic hydrolysis

Summary 1. The peptides from tryptic hydrolysis of triacetinase have been isolated and characterized and their amino-acid sequences have been determined.2. On the basis of the results of the determination of the amino-acid sequences of the peptides of the tryptic hydrolyzate the sequence of peptides of the cyanogen bromide hydrolysis of triacetinase has been established or confirmed.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 241–248, March–April, 1978.     

High-molecular-weight rRNAs of cotton seeds

The electrophoretic mobilities of the 25S and 18S rRNAs of cotton seeds in polyacrylamide gel have been studied. A pyrimidyl-RNase hydrolysate of the high-molecular-weight rRNAs was separated into isopleths containing up to decanucleotides. The mono-, di-, and trinucleotide isopleths were separated, respectively, into CP and Up; ApCp, GpCp, ApUp, and GpUp; ApApCp, GpApCp, ApGpCp, ApApUp, GpGpCp, ApGpUp + GpApUp, and GpGpUp on a KhZh 1305 microcolumn liquid chromatograph.     

Minor phospholipids of cotton seeds

Summary The minor components of the total PLs of seeds of the cotton plant of variety 108-F have been studied.N-Acylphosphatidylethanolamine and N-acyllysophosphatidylethanolamine have been isolated from cotton seed for the first time and some of their physicochemical properties and their fatty-acid compositions have been studied.Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 580–583, September–October, 1976.     

High-molecular-weight rRNAs of cotton seeds

The electrophoretic mobilities of the 25S and 18S rRNAs of cotton seeds in polyacrylamide gel have been studied. A pyrimidyl-RNase hydrolysate of the high-molecular-weight rRNAs was separated into isopleths containing up to decanucleotides. The mono-, di-, and trinucleotide isopleths were separated, respectively, into CP and Up; ApCp, GpCp, ApUp, and GpUp; ApApCp, GpApCp, ApGpCp, ApApUp, GpGpCp, ApGpUp + GpApUp, and GpGpUp on a KhZh 1305 microcolumn liquid chromatograph.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 746–750, November–December, 1982.     

Proteinase of germinated cotton seeds

A scheme has been developed to isolate and purify proteinase D from 3-day germinated cotton seeds. The physicochemical properties and substrate specificity were studied. It is found that cysteinic proteinase D cleaves auxiliary proteins to low-molecular-weight peptides and free amino acids.S. Yu. Yunusov Institute of the Chemistry of Plant Substances. Academy of Sciences of the Republic of Uzbekistan. Tashkent, fax (99871) 120 64 75. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 249–251, May–June, 2000.     

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.     

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.