THE AMINO ACID SEQUENCE OF MYOGLOBIN FROM THE MOLLUSC Aplysia limacina
- 1 July 1973
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 5 (4) , 187-200
- https://doi.org/10.1111/j.1399-3011.1973.tb03452.x
Abstract
The amino acid sequence of the globin prepared from the myoglobin contained in the radular muscle of the gasteropod mollusc Aplysia limacina was determined.According to the results thus obtained, the polypeptide chain of Aplysia limacina myoglobin is composed of 145 amino acid residues, in good agreement with the overall number of amino acid residues contained in the polypeptide chain of the vertebrate myoglobins studied to date. A particularly interesting feature of the myoglobin studied appears to be the presence in its polypeptide chain of only one histidine which occupies the 95th position.Keywords
This publication has 44 references indexed in Scilit:
- Abnormal human haemoglobins: I. The comparison of normal human and sickle-cell haemoglobins by “fingerprinting”Published by Elsevier ,2003
- Denaturation of Aplysia myoglobin. Equilibrium studyJournal of Molecular Biology, 1972
- Primary structure of N‐terminal part of molecule of dolphin myoglobinFEBS Letters, 1971
- Primary structure of aplysia myoglobin: Sequence of a 63‐residue fragmentFEBS Letters, 1971
- Structure of some peptides isolated from chymotryptic digest of dolphin myoglobinFEBS Letters, 1968
- Reversible thermal denaturation of Aplysia myoglobinJournal of Molecular Biology, 1968
- On proteins. CXV. Peptides isolated from chymotryptic digest of dolphin myoglobinCollection of Czechoslovak Chemical Communications, 1968
- Action of N-bromosuccinimide on human hemoglobin and its possible bearing on heme-globin linkageBiochimica et Biophysica Acta, 1963
- An improved method for the fingerprinting of human hemoglobinBiochimica et Biophysica Acta, 1961
- Studies on the structure of hemoglobin I. Physicochemical properties of human globinBiochimica et Biophysica Acta, 1958