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1. Amino acid sequences around the cystine residues in horse growth hormone

Author

Louise Oliver and Anne Stockell Hartree

Subjects
Electrophoresis, History, Chromatography, Paper, Cystine, Biology, Growth hormone, Education, chemistry.chemical_compound, Species Specificity, Endopeptidases, Animals, Chymotrypsin, Humans, Trypsin, Amino Acid Sequence, Horses, Amino Acids, chemistry.chemical_classification, Genetics, Horse, Articles, Pepsin A, Computer Science Applications, Amino acid, chemistry, Biochemistry, Growth Hormone, Cattle, Imines, Peptides
Abstract

The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.

Published
1968

2. [Covalent structure of horse myoglobin]

Author

M, Dautrevaux, Y, Boulanger, K, Han, and G, Biserte

Subjects
Cyanides, Chromatography, Paper, Myoglobin, Carboxypeptidases, Bromine, Chromatography, Ion Exchange, Pepsin A, Globins, Species Specificity, Genetic Code, Animals, Chymotrypsin, Amino Acid Sequence, Cetacea, Horses, Amino Acids, Peptides
Published
1969

3. Primary structures of the proinsulin connecting peptides of the rat and the horse

Author

H S, Tager and D F, Steiner

Subjects
Aspartic Acid, Alanine, Chemical Phenomena, Ethanol, Proline, Glycine, Carboxypeptidases, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Rats, Chemistry, Glutamates, Solubility, Species Specificity, Chromatography, Gel, Animals, Chymotrypsin, Electrophoresis, Paper, Amino Acid Sequence, Horses, Amino Acids, Peptides, Pancreas, Thiocyanates, Proinsulin
Published
1972

4. Structure covalente de la myoglobine de cheval.

Subjects
MYOGLOBIN, HEART, AMINO acids, PEPTIDES, HYDROLYSIS, CHYMOTRYPSIN, HORSES
Abstract

The complete sequence (153 amino acids) of horse heart myoglobin has been established. The sequence of a peptide isolated from chymotrypsin hydrolyzates of globin allowed to fill a gap in the tentative sequence previously proposed; this peptide was studied by means of pepsin hydrolysis, action of N-bromosuccinimide on histidyl bonds, and Edman degradation method associated with dansylation. After hydrolysis of globin by chymotrypsin treated by TLCK, the same major peptides were found as after hydrolysis by non-treated chymotrypsin. These peptides were identified by ionexchange resins and bidimensional paper chromatography, and also by the determination of their amino-acid composition. The suppression of secondary cuts explains the presence of new peptides, whose the composition and N-terminal Sequences were determined, it was then possible to confirm several sequences which could be previously deduced from the study of split products after cyanogen bromide treatment. The specificity of chymotrypsin towards certain types of peptide bonds is discussed. Horse myoglobin, as compared with sperm whale myoglobin, contains 18 differences: 17 substitutions and one inversion. The major part of the substitutions are located ih N- and C-terminal sequences: they are all punctiform, resulting from the replacement of only one base in each codon. [ABSTRACT FROM AUTHOR]

Published
1969
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