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563 results on '"Crotoxin"'

551. Amino-acid Composition of Crotoxin

Author

Primosigh J and Slotta Kh

Subjects
chemistry.chemical_classification, Multidisciplinary, Methionine, biology, Venoms, Cystine, Crotalus, Crotoxin, biology.organism_classification, Amino acid, chemistry.chemical_compound, chemistry, Amino acid composition, Biochemistry, Crotalid Venoms, Animals, Amino Acids
Abstract

THE first snake-venom prepared in the pure crystalline form was crotoxin from Crotalus terr. terr. as described in 1938; at that time only its cystine and methionine contents were quantitatively determined1. This protein, with a molecular weight of 30,0002, proved to be homogeneous3 in the ultra-centrifuge2 as well as by electrophoresis4.

Published
1951

552. Cloning and sequencing of cDNAs encoding the two subunits of Crotoxin

Author

Christiane Bouchier, Jean-Claude Boulain, André Ménez, Frédéric Ducancel, Cassian Bon, and Gilberte Guignery-Frelat

Subjects
Cloning, Genetics, Base Sequence, Protein subunit, Molecular Sequence Data, Neurotoxins, Nucleic acid sequence, Chromosome, Snakes, DNA, Molecular cloning, Biology, Crotoxin, chemistry.chemical_compound, chemistry, Complementary DNA, Crotalid Venoms, Animals, Amino Acid Sequence, Cloning, Molecular, Peptide sequence
Published
1988

554. Electron imaging of crotoxin complex thin crystal at 3.5 A.

Author

Jeng TW, Chiu W, Zemlin F, and Zeitler E

Subjects
Animals, Computers, Crystallography, Microscopy, Electron, Snakes, Crotalid Venoms analysis, Crotoxin
Abstract

Crotoxin complex forms thin crystals which are suitable for electron crystallographic analysis. We have used a 100 kV electron microscope equipped with a superconducting lens to image this crystal embedded in glucose. Optical diffraction analysis of the micrographs show unambiguously a structural resolution of 3.9 A which has not been obtained with the conventional microscope at room temperature. A density map with a nominal resolution of 3.5 A has been synthesized from these images by computer processing techniques.

Published
1984
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556. Experimental strategy in three-dimensional structure determination of crotoxin complex thin crystal.

Author

Jeng TW and Chiu W

Subjects
Animals, Crystallography methods, Freezing, Microscopy, Electron methods, Protein Conformation, Snakes, Crotalid Venoms, Crotoxin
Abstract

Electron images and diffraction patterns of crotoxin complex thin crystals contain high-resolution structural information in projection at both room and low temperatures. This paper outlines our strategy for collecting three-dimensional amplitude and phase data from these uniquely well-ordered toxin thin crystals. Preliminary experiments in support of the feasibility of this approach are presented.

Published
1984
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557. Specimen preparative methods for electron crystallography of soluble proteins.

Author

Cohen HA, Jeng TW, Grant RA, and Chiu W

Subjects
Animals, Crotoxin, DNA-Binding Proteins, Freezing, Glucose, Immunoglobulin Fc Fragments, T-Phages ultrastructure, Viral Proteins, Water, Crystallography methods, Microscopy, Electron methods, Proteins
Abstract

Technical factors which influence the choice of specimen preparation method for electron crystallographic study of thin crystals of soluble proteins are discussed. Ice embedding appears to be the most desirable choice of preparation method. However, in terms of the yield of major structural information, we conclude that negative stain remains a useful method for low resolution and glucose embedding for high resolution.

Published
1984
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