Back to Search
Start Over
Nature of Adenosine Triphosphatase Accelerating Peptide from Hydrolysate of Fur Seal Muscle
- Source :
- The Journal of Biochemistry. 86:1759-1764
- Publication Year :
- 1979
- Publisher :
- Oxford University Press (OUP), 1979.
-
Abstract
- Ultrafiltered fur seal muscle hydrolysate was divided into eleven fractions by gel filtration on Sephadex G-15. One of the fractions (Fraction G9) accelerated the ATPase activity of carp myosin B to a rate about two-fold faster than that of the control. Fraction G9 showed a single ninhydrin spot in its silica gel thin layer chromatograph, and gave a positive test for tryptophan by the p-dimethylaminobenzaldehyde method, while tests for tyrosine, and for arginine were negative. The ion exchange amino acid analysis of its acid hydrolysate showed a predominant content of lysine, nearly equivalent to the amount of tryptophan determined from its UV absorbancy and the p-dimethylaminobenzaldehyde method. The N-terminal amino acid analysis gave di-DNP-Lys as the sole DNP-amino acid. The structure of the ATPase accelerating peptide fraction, Fraction G9, was deduced to be Lys-Trp.
- Subjects :
- Carps
Arginine
ATPase
Lysine
Peptide
Myosins
Biochemistry
Hydrolysate
chemistry.chemical_compound
Animals
Molecular Biology
Adenosine Triphosphatases
chemistry.chemical_classification
biology
Fur Seals
Muscles
Tryptophan
Dipeptides
General Medicine
Caniformia
Enzyme Activation
Kinetics
chemistry
Sephadex
Ninhydrin
biology.protein
Spectrophotometry, Ultraviolet
Subjects
Details
- ISSN :
- 17562651 and 0021924X
- Volume :
- 86
- Database :
- OpenAIRE
- Journal :
- The Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....7130ecf6cb86b78cd97d0633794bf06b