Electrophoretic and amino acid compositions of the proteins of maize lines differing in the anthocyan coloration of the seeds

The electrophoretic and amino acid compositions of the proteins of lines of maize differing in the anthocyan coloration of their seeds have been investigated. The molecular masses of the quantitatively main components ranged from 11 to 42 kDa for the albumins and from 15 to 81 kDa for the globulins. Differences between the lines were observed in the levels of components with molecular masses of from 11 to 31 kDa. The amino acid compositions of the zeins of the lines studied were characterized by high levels of leucine, glutamic acid, aspartic acid, alanine and serine, and those of the other groups of proteins by high levels of arginine, glutamic acid, and glycine.Institute of Genetics, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 64 22 30. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 871–873, November–December, 1997.     

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, purification, and characterization of two forms of lipase from the fungusMucor miehei

Two forms of lipases (A and B) have been isolated from the fungusMucor miehei UzLT-3 and purified to the homogeneous state, and molecular masses of 43 and 40 kDa have been established for them from the results of disk electrophoresis and gel filtration. The isoelectric points of the lipases are 4.7 for form A and 4.9 for form B.Institute of Microbiology, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 41 71 29. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 673–676, September–October, 1994.     

Analysis of the nerve growth activities of protein fractions from the venoms of Agkistrodon halys halys and Echis multisquamatus

The possibility has been shown of obtaining NGFs in the process of isolating coagulant proteinases and other biologically active substances from the venoms of theAgkistrodon halys halys and theEchis multisquamata. Results characterizing the NGFs of both species as basic (weakly basic) proteins with molecular masses of 30.0–40.0 kDa are presented.Institute of Biochemistry, Uzbekistan Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 266–270, March-April, 1992.     

Isolation of β-(1→4)-glucan synthetase from cottonplant shoots

An enzyme complex including -(14)-glucan synthetase has been isolated from cottonplant shoots by chromatography and electrophoresis. Accrding to electrophoretic analysis under denaturing conditions, the molecular masses of the polypeptides presumably present in in the glucan synthetase complex amounted to 74, 50, and 30 kDa.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 87–90, January–February, 1994.     

Comparative study of the physicochemical properties of the species-specific proteins of cotton plants of the speciesGossypium hirsutum andG. barbadense

Four species-specific proteins have been isolated for the first time: H.0.43 and H.0.51 from aG. hirsutum cotton plant, and B.0.37 and B.0.48 fromG. barbadense. The conditions are given for their separation on Sephadex G-100 and on DEAE-cellulose and for their preparative electrophoresis in PAAG. Their isoelectric points and molecular masses have been determined and their subunit compositions have been investigated.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. 6, pp. 871–877, November-December, 1995. Original article submitted May 15, 1995.     

Stereospecificity of a lysophospholipase from the venom ofVespa orientalis

Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 89 14 75. Institute of Physiology and Biophysics, Academy of Sciences of the Republic of Uzbekistan, 700095, Tashkent, ul. Niyazova, 1. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 625–627, July–August, 1995. Original article submitted November 9, 1994.     

Isolation and some properties of glucose isomerase from a hybrid strain ofStreptomyces atratus

A highly effective easily reproducible method of obtaining high purity preparations of glucose isomerase from initial and hybrid strains of Streptomyces atratus has been developed. Two enzymes have been characterized, with molecular masses of 160 and 120 kDa, isoelectric points of 5.2 and 5.0, pH optima of 8.0 and 9.0, and temperature optima of 80 and 90°C, respectively. The activity of glucose isomerase preparations obtained by purification from a hybrid strain of Streptomyces atratus was 60–70% greater than that of analogous preparations from the initial parental strain.Institute of Microbiology of the Academy of Sciences, Republic of Uzbekistan, Tashkent, fax (3712) 417129 Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 903–907, November–December, 1996. Original article submitte March 11, 1996.     

Thin-layer chromatography of the sericin,fatty waxes,and fibroin of natural silk

The method of thin-layer and high-performance thin-layer chromatography is proposed for the investigation of the isolation of sericin, fatty waxes, and fibroin from a natural silk cocoon. The chromatographic fractionation of fibroin according to molecular masses has been studied.Institute of the Chemistry and Physics of Polymers, Academy of Sciences of the Republic of Uzbekistan, Tashkent. fax (3712) 44 26 61. Translated from Kbimiya Prirodnykh Soedinii, No. 4,pp. 588–590, July–August, 1995. Original article submitted October 17, 1994.     

Lipids of the biomass ofRuta graveolens, grownin vivo andin vitro

A lower content of chlorophylls, phospholipids, and linolenic acid and a higher content of rutin, carotenoids, and xanthophylls in the biomass ofRuta graveolens L. obtainedin vitro has been found as compared with these indices from the epigeal part of the plant grownin vivo.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent. Institute of Botany, Academy of Sciences of the Republic of Uzbekistan, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 651–655, September–October, 1993.     

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.     

Enzyme peroxidase in calluses of cotton plants of the speciesGossypium hirsutum andG. herbaceum

A comparative study has been made of the activity of the enzyme peroxidase and its isozyme spectrum from two species of cotton plant. It has been found that, as calluses grow, new isoforms of peroxidase are produced and the protein content increases.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, fax 627071. Institute of Genetics, Academy of Sciences of the Republic of Uzbekistan, fax 642230. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 90–92, January–February, 1994.     

Amino acid and fractional compositions of the protein fractions of the biomass of micromycetes and their biological value

On the basis of the results of an investigation of cellulolytically active micromycetes the full value and balanced nature of their protoplasmic proteins have been shown.Institute of Microbiology, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 41 71 29. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 385–389, May–June, 1999.     

Carbohydrates of cultivated varieties ofAlthea rosea

The polysaccharides of three cultivated varieties ofAlthea rosea have been investigated. The amounts of water-soluble polysaccharides and pectin substances in various organs of the plant have been determined. It has been shown that the maximum amount of water-soluble polysaccharides and pectin substances is present in the flowers. Their monosaccharide compositions have been studied. The physicochemical characteristics of the pectin substances are given.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Republic of Uzbekistan, Tashkent. A. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan. Tashkent. Institute of Botany, Academy of Sciences of the Republic of Uzbekistan, Tashkent. Translated from Khimiya Prirodnykh Soedineii, No. 5, pp. 643–646, September–October, 1993.     

Quantitative determination of the main component of the pheromone of the beet army worm moth as a function of the time of day influence of a brain extract on the induction of the pheromone

A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 137–139, January–February, 1994.     

Comparative characteristics of proteins of cottonplant lines differing in the strength of the fiber

The enzymes and proteins of the fibers of two lines of cotton plant differing in the strength of the fiber have been investigated. It has been shown that the activities of glucan synthetase and peroxidase rise as the fiber matures, while the activities of β-(1-3)-glucanase and cellulase fall. The specific enzymatic activities of peroxidase and glucan synthetase in the L-175 line, distinguished by a stronger fiber, are higher than for the L-466 line with a weaker fiber. The activity of glucanase changes according to the strength of the fiber. In a study of the protein composition of cotton fibers, polypeptides with molecular masses of 28 and 39 kDa were found among the proteins responsible for the strength of the fiber. A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax (3712) 162 70 71. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 530–536, July–August, 1998.     

Biochemical characteristics of the cholinesterase of the turnip mothAgrotis segetum

A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 141–142, January–February, 1994.     

Arenobufagin and gamabufotalin from the venom of the Central Asian toadBufo viridis

A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 140–141, January–February, 1994.     

An investigation of the venom of the spiderSegestria florentina as a blocker of the catalytic activities of esterases

A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 133–134, January–February, 1994.     

An investigation of the membranotropicity of the ethylene- and cytokinin-binding proteins from cottonplant shoots by the fluorescent probe method

A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of Uzbekistan, Tashkent, fax 627071. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 135–136, January–February, 1994.