Myoglobins of Cartilaginous Fishes. II. Isolation and Amino Acid Sequence of Myoglobin of the Shark Mustelus Antarcticus
| Autor: | Thompson Eo, Koureas Dd, Fisher Wk |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Magnetic Resonance Spectroscopy
Size-exclusion chromatography Peptide Mass Spectrometry chemistry.chemical_compound Residue (chemistry) Endocrinology Genetics medicine Animals General Materials Science Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification biology Myoglobin General Medicine Chromatography Ion Exchange biology.organism_classification Peptide Fragments Heterodontus portusjacksoni Carboxymethyl cellulose Reproductive Medicine Biochemistry chemistry Vertebrates Chromatography Gel Sharks Animal Science and Zoology Mustelus antarcticus Developmental Biology Biotechnology medicine.drug |
| Zdroj: | Australian Journal of Biological Sciences. 33:153 |
| ISSN: | 0004-9417 |
| DOI: | 10.1071/bi9800153 |
| Popis: | Myoglobin isolated from red muscle of the gummy shark M. antarcticus was purified by gel filtration and ion-exchange chromatography on carboxymethyl cellulose in 8 M urea-thiol buffer. Amino acid analysis and sequence determination showed 148 amino acid residues. The amino terminal residue is acetylated as shown by nuclear magnetic resonance and mass spectrographic analysis of an N-terminal peptide. There is a deletion of four residues at the amino terminal end as well as one residue in the CD interhelical area relative to other myoglobins. These overall differences were also found previously in myoglobin of Heterodontus portusjacksoni. The complete amino acid sequence has been determined following digestion with trypsin, chymotrypsin, thermolysin, staphylococcal protease and cyanogen bromide. Sequences of purified peptides were determined by the dansyl-Edman procedure. The amino acid sequence showed approximately 88 differences from mammalian, monotreme, bird and tuna myoglobins, slightly more than previously reported for H. portusjacksoni usually considered a more primitive animal. There were 24 residues common to both shark myoglobins that were different from those present in other myoglobins. The sequence has been compared to the myoglobin of yellowfin tuna and other myoglobins. |
| Databáze: | OpenAIRE |
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