scholarly journals Amino Acid Sequence of the a-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc Anadara Trapezia

1980 ◽  
Vol 33 (6) ◽  
pp. 653 ◽  
Author(s):  
PF Como ◽  
EOP Thompson
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Magnetic Resonance ◽  
Amino Acid Sequence ◽  
Bivalve Mollusc ◽  
Amino Terminus ◽  
Spectrographic Analysis ◽  
Amino Acid Residues ◽  
Amino Terminal ◽  
A Chain

The amino acid sequence of the IX-chain of the tetrameric haemoglobin of the bivalve mollusc A. trapezia shows 153 amino acid residues, longer than invertebrate globins previously sequenced. The amino terminal residue is acetylated as shown by nuclear magnetic resonance and mass spectrographic analysis of an N-terminal peptide. There are additional residues at the amino terminus, similar to the IX-globin of the shark and lamprey globin. In common with other invertebrate globin sequences, when compared with vertebrate globins it is necessary to insert extra gaps in interhelical regions of the vertebrate alignment to preserve homology.

Myoglobin of the Shark Heterodontus Portusjacksoni: Isolation and Amino Acid Sequence

1979 ◽  
Vol 32 (3) ◽  
pp. 277 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Spectrographic Analysis ◽  
Amino Acid Residues ◽  
Sequence Determination ◽  
Amino Terminal ◽  
Red Muscle

Myoglobin isolated from red muscle of the shark H. portusjacksoni was purified by ion-exchange chromatography on sulfopropyl-Sephadex and gel-filtration. Amino acid analysis and sequence determination showed 148 amino acid residues. The amino terminal residue is acetylated as shown by mass spectrographic analysis of N-terminal peptides. 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.

scholarly journals Haemoglobins of the Shark, Heterodontus Portusjacksoni II. Amino Acid Sequence of the a-Chain

1976 ◽  
Vol 29 (2) ◽  
pp. 73 ◽  
Author(s):  
AR Nash ◽  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Chromatography ◽  
Cyanogen Bromide ◽  
Gel Filtration ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Amino Terminal ◽  
Core Peptide ◽  
A Chain

The amino acid sequence of the a-chain of the principal haemoglobin from the shark, H. portusjacksoni has been determined. The chain has 148 residues and is acetylated at the amino terminal. The soluble peptides obtained by tryptic and chymotryptic digestion of the protein or its cyanogen bromide fragments were isolated by gel filtration, paper ionophoresis and paper chromatography. The amino acid sequences were determined by the dansyl-Edman procedure. The insoluble 'core' peptide from the tryptic digestion contained 34 residues and required cleavage by several proteases before the sequence was established. Compared with human a-chain there are 88 amino acid differences including the additional seven residues which appear on the amino terminal of the shark chain. There is also one deletion and one insertion. The chain contains no tryptophan but has four cysteinyl residues which is the highest number of such residues recorded for a vertebrate globin.

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