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Start Over Topic chymotrypsin Topic horses Publication Year Range More than 50 years ago
11 results

1. Trypsin inhibitors and chymotrypsin inhibitors in the sera of some animals

Author

Shojiro Nakamura, Hatanori Ogata, and Ryosuke Suzuno

Subjects
Ranidae, Physiology, Swine, Trypsin inhibitor, Guinea Pigs, Cyprinidae, Paper electrophoresis, Biochemistry, Guinea pig, Hydrolysis, Dogs, Species Specificity, Alpha-Globulins, medicine, Animals, Chymotrypsin, Humans, Electrophoresis, Paper, Horses, Carp, Molecular Biology, Rana catesbeiana, Sheep, biology, Horse, General Medicine, Blood Proteins, biology.organism_classification, Trypsin, Anguilla, Rats, Turtles, Enzyme Activation, biology.protein, Cats, Cattle, Rabbits, Anura, Trypsin Inhibitors, medicine.drug
Abstract

1. 1. The sera of human, cattle, sheep, pig, horse, rabbit, rat, guinea pig, dog, cat, tortoise, frog, bull frog, carp, and eel were separated on paper electrophoresis. The localization of trypsin and chymotrypsin inhibitors were observed with the serum protein fractions, using anilide substrates. 2. 2. The localization curves were compared with the cross diagrams of the sera against trypsin and chymotrypsin, except tortoise. 3. 3. Bovine α2-globulin fraction was found to activate the hydrolysis of benzyol - spl - tryosine -p- nitroanilide by chymotrypsin.

Published
1972

2. Primary structure of cytochrome c from the elephant seal, Mirouga leonina

Author

Max A. McDowall, Robert C. Augusteyn, Burt Zerner, and Edwin C. Webb

Subjects
Chromatography, Paper, Swine, Carboxypeptidases, Biochemistry, Genetics and Molecular Biology (miscellaneous), Leucyl Aminopeptidase, Dogs, Species Specificity, Elephant seal, Animals, Chymotrypsin, Electrophoresis, Paper, Trypsin, Amino Acid Sequence, Horses, Amino Acids, Peptide sequence, Leucyl aminopeptidase, Dansyl Compounds, Chromatography, biology, Cytochrome c, Myocardium, Protein primary structure, biology.organism_classification, Chromatography, Ion Exchange, Pepsin A, Caniformia, Paper chromatography, Biochemistry, biology.protein, Chromatography, Gel, Cytochromes, Isoleucine, Peptides
Abstract

Twenty-seven peptides, including the haemopeptide, were isolated from a single chymotryptic digest of seal heart cytochrome c by chromatography on Sephadex G-75, Whatman phosphocellulose P-70 and Bio-Rad AG 50W-X2. These peptides were purified by electrophoresis or chromatography on paper and their sequences were determined. The complete sequence of the protein was deduced by alignment of these peptides by comparison with the known sequences of several other cytochromes c. Seal cytochrome c differs from the dog and horse proteins in 1 and 6 positions, respectively. The single difference from dog cytochrome c is found in position 100 where isoleucine, in the seal, replaces the lysine found in the dog.

Published
1972

3. Kinins released from horse heat-acid-denaturated plasma by plasmin, plasma kallikrein, trypsin and Bothrops kininogenase

Author

Olga B. Henriques and Elvira Gapanhuk

Subjects
Electrophoresis, Protein Denaturation, Hot Temperature, Chemical Phenomena, Chromatography, Paper, Plasmin, Guinea Pigs, Bradykinin, Kinins, Acetates, Biochemistry, chemistry.chemical_compound, Methionine, Ileum, medicine, Animals, Chymotrypsin, Trypsin, Fibrinolysin, Horses, Pharmacology, Chromatography, biology, Venoms, Chemistry, Kallidin, Lysine, Horse, Snakes, Kallikrein, biology.organism_classification, Blood, Chromatography, Gel, Bothrops, Biological Assay, Kallikreins, Peptide Hydrolases, circulatory and respiratory physiology, medicine.drug
Abstract

Isolation and identification of kinins released from heat-acid-denaturated horse plasma by plasmin, plasma kaliikrein, trypsin and Bothrops kininogenase was carried out. From heat-acid-denaturated plasma, plasmin released mainly methionyllysyl-bradykinin and small amounts of bradykinin and kallidin. Plasma kallikrein released only bradykinin from this substrate. Trypsin released mainly bradykinin and kallidin, and traces of methionyl-lysyl-bradykinin. Bothrops kininogenase released mainly bradykinin, but some kallidin was also found in the substrate-enzyme incubate.

Published
1970

4. 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

5. Dissociation and recombination of the subunits of the cholera enterotoxin (choleragen)

Author

R A, Finkelstein, M, Boesman, S H, Neoh, M K, LaRue, and R, Delaney

Subjects
Immunodiffusion, Autoanalysis, Immune Sera, Administration, Oral, Sodium Dodecyl Sulfate, Electrophoresis, Disc, Enterotoxins, Chromatography, Gel, Animals, Chymotrypsin, Electrophoresis, Paper, Electrophoresis, Polyacrylamide Gel, Trypsin, Horses, Rabbits, Amino Acids, Peptides, Vibrio cholerae, Skin Tests
Published
1974

7. [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

9. 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

10. 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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11. Horse Liver Alcohol Dehydrogenase.

Author

Jörnvall, Hans

Subjects
DEHYDROGENASES, LIVER, ALCOHOL, HORSES, CHYMOTRYPSIN, CYANOGEN compounds, PEPTIDES
Abstract

1. The ethanol-active isoenzyme of horse liver alcohol dehydrogenase has been carboxymethylated with iodo[14C]acetate and different samples of the labelled protein treated with trypsin (both with and without previous maleylation of the substrate), chymotrypsin, pepsin or cyanogen bromide. In each case most of the resultant peptides have been purified and characterized. 2. Data are given for those peptides originating from an N-terminal region comprising about 40% of the protein chain and the amino acid sequence of the first 140 residues is deduced. 3. It is established that over this region the two chains of the enzyme have an identical sequence. The N-terminus is an acetylated serine residue and the "active site" cysteine residue occupies position no. 46. One of the two tryptophans of the chain, but none of the four tyrosines, is in the sequence given. The region around position 100 is rich in cysteine residues. Some serine residues were found to have reacted during maleylation of the protein. 4. The amino acid sequence is compared to the previously known sequences of glyceraldehyde 3-phosphate dehydrogenase from two species. Similarities strongly suggest a true homology, at least of an N-terminal region, and support theories of a common ancestral origin for these enzymes. The reactive cysteine residues are, however, at widely different positions in the primary structures. [ABSTRACT FROM AUTHOR]

Published
1970
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