Change in the activity of the proteolytic enzymes of cotton seeds when the plants are affected by wilt

The change in the proteolytic activity of the seeds of the cotton plant varieties Tashkent-1- Tashkent-6, S-4727, and 108-F when the plants are affected by wilt has been studied. A relationship has been established between the decrease in activity for seeds of the Tashkent-1 and Tashkent-6 varieties and the degree of attack by wilt. A hypothesis has been put forward on the existence of variety differences in the response reaction of the cotton plant to the introduction of the pathogen. The appearance of distinctive electrophoretic protein components in the seeds of wilt-affected cotton plants of the Tashkent-1 and Tashkent-6 varieties has been shown. A hypothesis has been made of a possible increase in the amount of proteinase inhibitors in response to the infection of the plants by wilt, a consequence of which is a sharp decrease in proteolytic activity and the appearance of distinctive electrophoretic components.Institute of Chemistry of Plant Substances of the Uzbek Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 704–708, September–October, 1987.     

Lipolytic activities of enzymes in cotton seeds

Chemistry of Natural Compounds -     

Characteristics of the lipolytic enzymes of cotton seeds

Chemistry of Natural Compounds -     

Functions of inhibitors of proteolytic enzymes in plants

The literature on proteinase inhibitors of plant origin over the last 15 years is discussed. The results of investigations are permitting an expansion of our ideas on the regulatory and protective functions of proteinase inhibitors, which play a primary role in the resistance of plants to phytopathogens and can be used as a test in selection practice.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, Vol. 33, No. 1, pp. 42–48, January–February, 1997.     

Lipid composition of the seeds of the cotton plant infected with wilt

The qualitative and quantitative set of lipid components of the seeds of healthy cotton plants of the variety Tashkent-1 and plants infected with verticillium wilt have been studied. It has been established that the compositions of the lipids of the two samples differ considerably. The greatest differences are observed in the amounts of total lipids, gossypol, and low-molecular-weight volatile acids.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 319–325, May–June, 1980.     

Lipolytic enzymes of cotton seeds V. Triacetinase

Chemistry of Natural Compounds - 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...     

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.     

Lignin of the fine-fibered cotton plant of variety S-6030 affected by fusarial wilt. II

A comparative study of the products of cleavage by sodium in liquid ammonia of the dioxane lignins (DLAs) from healthy and fusarial-wilt-affected stems of the fine-fibered cotton plant of variety S-6030 and a study of the PMR spectra of both lignins has shown that the DLA from the healthy stems is more highly condensed than the DLA of the stems affected by wilt. The main structures of DNA wilt are of the guaiacyl type. In the DLA from the affected stems, the amount of p-coumaryl structures had increased, which confirms the demethylating action of fusarial wilt on cotton-plant lignin.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 364–366, May–June, 1986.     

Study of the lipolytic enzymes of cotton seeds IV. Triacetinase

Summary A triacetinase with mol. wt. 36,000 has been isolated from cotton seeds by ion-exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-100.The homogeneity of the protein has been confirmed by the results of rechromatography and ultracentrifugation.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 628–632, September–October, 1974.     

Immunochemical characterization of a proteolytic enzyme — Protease A from cotton seeds

It has been established by double immunodiffusion in agar that protease A (a proteolytic enzyme from dormant cotton seeds hydrolyzing the native reserve proteins) is present for the first 3–4 days during the germination of the seeds. An immunological affinity between trypsin and protease A has been revealed which indicates the presence of common structural elements in them.Institute of Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 109–110, January–February, 1991.     

Isolation and study of an inhibitor of the intrinsic proteolytic enzyme of cotton seeds

A scheme has been developed for the isolation of an inhibitor of cottonseed protease A using affinity chromatography on protease-A—Sepharose 4B followed by gel filtration on Sephadex G-150. The molecular mass of the inhibitor is 20 kDa. The protein molecule consists of two subunits with different molecular masses.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent, Fax (3712) 62 73 48. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 274–277, March–April, 1994.     

Isolation and study of an inhibitor of the intrinsic proteolytic enzyme of cotton seeds

A scheme has been developed for the isolation of an inhibitor of cottonseed protease A using affinity chromatography on protease-A—Sepharose 4B followed by gel filtration on Sephadex G-150. The molecular mass of the inhibitor is 20 kDa. The protein molecule consists of two subunits with different molecular masses.     

The lignin of the sea island cotton plant of variety S-6030 affected by fusarial wilt. I

A comparative study of the dioxane lignins isolated from healthy and wilt-affected cotton plant stems has shown thatFusarium fungi demethylate lignin and make it more oxidized than the lignin from healthy stems.     

The lignin of the sea island cotton plant of variety S-6030 affected by fusarial wilt. I

A comparative study of the dioxane lignins isolated from healthy and wilt-affected cotton plant stems has shown thatFusarium fungi demethylate lignin and make it more oxidized than the lignin from healthy stems.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 825–827, November–December, 1985.