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.     

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.     

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 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.     

Isolation of immunosimilar proteins from cotton seeds by immunoaffinity chromatograph

A sorbent highly specific forVerticillium proteins has been obtained from BrCN-Sepharose and rabbit immunoglobulins. By affinity chromatography using this sorbent a protein immunologically similar to the proteins of the mycelium of the fungusV. dahliae has been isolated from cotton seeds of the Tashkent-1 variety. The molecular mass of the protein has been determined, and its proteolytic activity has been established. Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 746–749, September–October, 1993.     

Isolation of immunosimilar proteins from cotton seeds by immunoaffinity chromatograph

A sorbent highly specific forVerticillium proteins has been obtained from BrCN-Sepharose and rabbit immunoglobulins. By affinity chromatography using this sorbent a protein immunologically similar to the proteins of the mycelium of the fungusV. dahliae has been isolated from cotton seeds of the Tashkent-1 variety. The molecular mass of the protein has been determined, and its proteolytic activity has been established.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 746–749, September–October, 1993.     

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.     

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.     

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.     

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.