A study of the mechanism of the action of extensin-like proteins of the cotton plant in a cell culture

The mechanism of the action of extensin-like proteins (ELPs) isolated from the cotton plant on a cell line of murine melanoma (CML) has been studied from the inclusion of³H-thymidine and by counting live cells. The dose- and phase-dependent inhibitory nature of the action of ELPs on MLC cells has been established.Deceased.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (371) 162 70 71. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 372–375, May–June, 1999.     

Action of cottonplant glycoproteins on the proliferative activity of cells

A mitogenic action of the total (LLPs) and lactose-specific (LLPs-1) lectin-like proteins on the proliferation of lymphocytes and of myeloma cells in culture has been found. A dose-dependent influence of the LLPs and extensin-like proteins (ELPs) on the inclusion of³H proteins in the myeloma cells, including an antimitotic effect of the ELPs with an increase in the protein dose, has been shown; the ELPs exert an analogous action on K–562 tumor cells of human erythroblasts. The nature of the biological action of the LLPs and ELPs is discussed in connection with features of the structure of the carbohydrate fragments of the composition of the glycoproteins.A. S. Sadykov Institute of Bioorganic Chemistry of the Academy of Sciences, Republic of Uzbekistan, Tashkent, fax (3712) 62 70 71. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 912–915, November–December, 1996. Original article submitted May 20, 1996.     

Isolation of a protein with diaphorase activity from cotton seeds and a study of some of its properties

The diaphorase activities of the proteins of different varieties of two species of cotton plant —Gossypium hirsutum L. andG. barbadense L. — have been studied. It has been shown that the proteins of the seeds of the cotton plantG. barbadense possess a low diaphorase activity in comparison with the proteins of the seeds of aG. hirsutum plant. On an electrophoretogram of the proteins, diaphorase activity was localized in two zones, with R_f 0.45 and 0.70. The diaphorase with R_f 0.45 has been isolated by electrophoresis in polyacrylamide gel (PAAG) and some of its properties have been studied. The diaphorase isolated oxidizes NADH and NADPH in the presence of various artificial electron Acceptors, and has two pH optima (at 7.20 and 8.70) and is characterized by relative thermal stability (at 80°C). In the case of the total extract, brief boiling does not lead to inactivation of the enzyme, which shows the presence in cotton seeds of a factor stabilizing this diaphorase. The molecular weight of the proteins isolated, according to gel filtration on Sephadex G-150, is 59,000, and from the results of SDS-PAAG electrophoresis it is 13,600, which shows a tetrameric structure of the enzyme.Institute of Experimental Plant Biology, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 416–421, May–June, 1987.     

Solubility of the proteins and phytates of cottonseed meal in the presence of metal ions

The solubility of the proteins and phytates of cotton seeds in the presence of metal ions (Ca²⁺, Fe³⁺, Zn²⁺) at various pH values of the medium has been studied. It has been shown that complete precipitation of the protein by phytin from solution (C_protein)=1.5%), sets in at a mass ratio of phytin to protein of 1:15, pH 1.5.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. 3, pp. 421–424. May–June, 1994.     

A study of the dioxane lignins of Althaea nudiflora and A. rosea

Summary 1. The lignin has been isolated from the stems of the cotton plant of a late period of vegetation by the hydrochloric acid method. The elementary composition and functional groups have been determined. The mean composition for a C₆-C₃ structural unit has been determined.2. By the oxidation of a powder of the stems of the cotton plant with nitrobenzene in the presence of alkali it has been established that the hydrochloric acid lignin is more condensed than the DLA.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 648–650, September–October, 1975.     

Composition of the phospholipids of Gossypium barbadense

Summary 1. The combined phospholipids of the seed kernels of the cotton plant have been completely freed from accompanying carbohydrates by gel filtration on Molselekt G-25.2. It has been established by two-dimensional chromatography in a thin layer of silica gel that the phospholipids of the seed kernels of the cotton plant of thin-fibered variety 5904-I consist of X₁- and X₂-polygly cerophosphatides (2.4 and 7.1%, respectively), phosphatidylethanolamines (14.1%), phosphatidylcholines (50.4%), phosphatidylinositols (20.4%), and lysophosphatidylcholines (5.6%).3. The accompanying substances of the phospholipids of the cotton plant form two groups each of steroids and disaccharides.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 19–21, January–February, 1976.     

A natural undecaprenol and its influence on the biochemical reactions of cotton seedling nuclei

A method has been developed for isolating polyprenols from the leaves of cotton plants of lines L-463, L-501, and L-4. The influence of an undecaprenol on the level of biosynthesis of the proteins of the nuclei of cotton seedlings has been studiedin vivo andin vitro. It has been found that they double the level of biosynthesis nuclear proteins when the seeds are first wetted in a 0.1% solution.Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 65–69, January–February, 1998.     

The change in the globulins during the development of cotton seeds

The biosynthesis of the 11S and 7S globulins — the main reserve proteins of cotton seeds — has been investigated. The periods at which the globulins appear in cotton seeds have been established. The changes in the amino acid composition and in the secondary structure of the 11S globulin during the ripening of cotton seeds have been studied.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. 349–355, May–June, 1984.     

Structure - Function Relationship of Extensin - Like Cotton Proteins

The structure-function relationship of extensin-like proteins (ELP) of cotton is studied by molecular modeling. The antiproliferative activity of deglycosylated ELP on a cell culture of KML murine melanoma is shown to be more expressed than the activity of the ELP themselves.     

Characteristics of the 5S rRNA from cotton seeds

The individuality of the 5S rRNA from cotton seeds has been determined by the production of a single narrow band on gel electrophoresis and by the characteristic UV spectrum with values of the ratios E₂₆₀/E₂₃₀ and E₂₆₀/E₂₈₀ of 2.03–2.1 and 2.08–2.14, respectively. The melting curve of the 5S rRNA has been obtained and a total hyperchromic effect of 25% has been calculated. The nucleotide composition of the 5S rRNA has been established by determining the amount of nucleotides in an alkaline hydrolysate (22.6% of AMP; 30.2% of GMP; 22.6% of UMP; and 24.6% of CMP). The nucleotides were identified from the position of their appearance in the elution profile, from their UV spectra in 0.1 N HC1 and 0.1 KOH, and also by one- and two-dimensional chromatography of the nucleotides obtained, in the presence of markers.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. 817–821, November–December, 1980.     

Study of the total histone of the cotton plant of variety 108-F

From two-day etiolated shoots of the cotton plant of variety 108-F we have isolated the total histone and purified it on a column of CM-cellulose. It has been shown by gel electrophoresis and amino acid analysis that the total histone of the cotton plant, like the total histone of wheat, consists of five main fractions, the amount of the lysine-rich fraction A₁ being greater in the cotton plant than in wheat (23% and 19%, respectively), and the amount of arginine-rich fraction A₄ being less (19.2 and 24.3%, respectively). The total histone of the cotton plant is less basic (ratio of basic amino acids to acidic amino acids in the cotton-plant histone 1.24, in wheat histone 1.9, and in calf thymus histone 1.78) but richer in lysine as compared with arginine than the histones of wheat and calf thymus.V. I. Nikitin Institute of Chemistry, Academy of Sciences of the Tadzhik SSR, Dushanbe. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 109–112, January–February 1980.     

Mass-spectrometric investigation of sterol and triterpenoid esters from leaves of the cotton plant

The qualitative composition of two fractions of extractive substances isolated from the leaves of a cotton plant of the variety 108-F and containing sterol and triterpenoid esters with saturated and unsaturated aliphatic acids having chain lengths of from C₁₂ to C₃₀ has been studied by a group of mass-spectrometric methods. A total of 45 compounds was detected.Institute of the Chemistry of Plant Substances, Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 208–215, March–April, 1990.     

Molecular composition of the N-acylphosphatidylethanolamine of the cotton plant of variety S-6029

An N-arylphosphatidylethanolamine has been isolated from the total phospholipids of the cotton plant of variety S-6029. The composition and the position distribution of the fatty-acid radicals has been studied with the aid of enzymatic hydrolysis with phospholipase A₁ (from the fungusRhisophus microsporus UzLT-1) and by alkaline and acid hydrolyses. From the results obtained, the possible molecular composition of the N-acylphosphatidylethanolamine has been calculated by Coleman's method. The total number of all the molecular species amounted to 720.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 780–783, November–December, 1979.     

A structural-functional study of cottonplant glycoproteins

The results are presented of a structural-functional investigation of two groups of cottonplant glycoproteins — lectin-like and extensin-like proteins — using the methods of molecular modeling of various structural fragments of the glycoproteins.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (371) 162 70 71. Translated fromKhimiya Prirodnykh Soedinenii, No. 3, pp. 376–384, May–June, 1999.     

A study of the lignin of the sea island cotton plant of variety S-6030

The dioxane lignin has been isolated by Pepper's method with a yield of 9.5% on the Komarov lignin from the ripe stems of the sea island cotton plant of variety S-6030. The developed emperical formula has been calculated, the IR and UV spectra have been taken, and the molecular-mass distribution has been studied. The dioxane lignin is polydisperse. M_w=10,100, M_n=5350.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 628–630, September–October, 1983.     

The flavonols of the flowers ofGossypium hirsutum L. (cotton variety 108-F)

Summary Quercimeritrin C₂₁H₂₀O₁₂, and a new flavonol glucoside with mp 228–230° and composition C₂₁H₂₀O₁₂, which has been shown to be quercetin 3-glucoside, have been extracted from flowers of the cotton variety 108-F.Khimiya prirodnykh soedinenii, Vol. 1, No. 1, pp. 67–70, 1965     

Comparative investigation of the molecular structures of the species-specific proteins of the seeds ofGossypium hirsutum andG. barbadense

The N-terminal amino acids and the amino acid compositions of four species-specific proteins of two species of the cotton plant —Gossypium hirsutum andG. barbadense — have been determined. Peptide maps of tryptic hydrolysates of these proteins have been obtained and compared. Individual tryptic peptides have been isolated and purified. The N-ends, amino acid compositions, and amino acid sequences of individual peptides have been determined. The N-terminal sections of the proteins ofG. hirsutum andG. barbadense as far as the 16th amino acid residue have been sequenced. A comparative analysis has been made of the peptides and proteins of these cottonplant species.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, No. 6, pp. 858–864, November–December, 1997.     

Phospholipids of the cotton plant of variety Tashkent-3. II. Structure of the main phospholipid fractions

Summary 1. Individual fractions of phosphatidylcholines, phosphatidylethanolamines, phosphatidylinositols, and the X₂ and X₃ phospholipids have been obtained from the combined phospholipids, freed from carbohydrates, of the seed kernels of the cotton plant of variety Tashkent-3.2. The compositions and position distributions of the fatty acids in the main fractions of phospholipids have been studied.3. The possible molecular composition of the phosphatidylcholines, phosphatidylethanolamines, and phosphatidylinositols have been calculated.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 155–158, March–April, 1976.     

Effect of Extensin - Like Cotton Proteins on Eukaryotic Cell Gene

The effect of extensin-like cotton proteins (ELP) on animal cell gene (KML cell culture) was studied. Cells perish (50%) at protein dose 100 g/mL (cytotoxic effect). DNA fragmentation is not observed. Cell death from ELP is hypothesized to occur via necrosis resulting from destruction of intracellular biochemical processes     

Electrophoretic investigation of the seed proteins of the cotton plantGossypium hirsutum

The proteins of the buffer-soluble fraction of the seeds of cotton plants of the speciesGossypium hirsutum, wild and ruderal varieties, have been investigated by electrophoresis in polyacrylamide gel and have been subdivided into two classes. Characteristic components have been detected in the protein spectra of these samples. In diploid species of the cotton plant, in addition to characteristic protein components, individual components are also observed.Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 736–738, September–October, 1995. Original article submitted November 21, 1994.