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M Coates

Publications and source records attributed to M Coates.

45 records · Page 3Linked to original sources
PubMed1977

alpha-chain sequence of newt haemoglobin (Taricha granulosa).

The amino acid sequence of the alpha-chain of the major haemoglobin of a newt, T. granulosa, has been determined. The chain is 142 residues long and has an extra methionine at its N-terminus when compared with human alpha-chain. Most of the tryptic peptides were sequenced by a combination of the subtractive Edman method and by deduction from the compositions of overlapping fragments produced by various enzymic treatments. The sequence of two 'core' regions was obtained by automatic sequencing of large peptides produced by trypsin cleavage at arginine residues only after blockage of lysine residues by citraconylation; by cleavage between aspartic acid and proline residues with 70% formic acid, and by cyanogen bromide cleavage at methionine residues. The sequence of T. granulosa alpha-chain is compared with those of representative species from the other classes of vertebrates. The differences in alpha-chain between the classes of vertebrates are compared with the differences in this protein between an equal number of orders of mammals. This comparison allows us to conclude that the major functional and conformational features of alpha-chain have been conserved since the divergence of the classes of jawed vertebrates.

Amino Acid Sequence↗
PubMed1975

Studies on the interaction of organic phosphates with haemoglobin in an amphibian (Bufo marinus), a reptile (Trachydosaurus rugosus) and man.

The primary organic phosphate modifiers of haemoglobin function are DPG (2,3-diphosphoglycerate) in the toad Bufo marinus and ATP in the lizard Trachydosaurus rugosus. Myo-IP6 (myo-inositol hexaphosphate) and myo-IP5 (myo-inositol pentaphosphate) are more effective than ATP or DPG in reducing the oxygen affinities of the haemoglobins of B. marinus, T. rugosus and man, while ATP and DPG are about equally effective. Competition experiments indicate that ATP, DPG and myo-IP6 bind to the same site or sites on the haemoglobins of each of the species. These findings, and those of others, are interpreted as evidence that the evolution of an organic phosphate binding site on the haemoglobin of an ancient vertebrate pre-adapted haemoglobin for interaction with a set of organic phosphates having certain structural features in common.

Adenosine Diphosphate↗
PubMed1971

Folie à deux.

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Humans↗