A structural and functional polymorphism in the hemoglobin O2 transport system of the blood clamNoetia ponderosa

✍ Scribed by Mangum, Charlotte P. ;Cockey, Elizabeth M.

• Publisher: John Wiley and Sons
• Year: 1993
• Tongue: English
• Weight: 442 KB
• Volume: 266
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402660412

✦ Synopsis

Abstract

A sample of arcid blood clams (Noetia ponderosa) from the Atlantic coast of Virginia had red blood cells containing a hemoglobin composed of only one electrophoretically separable component. Both the red blood cells and hemoglobin extracts had a moderately high oxygen affinity. A sample from the Gulf of Mexico had red blood cells containing hemoglobins composed of two components. According to previous reports, this population contains a homodimer of one chain and a heterodimer of that chain plus another. Both the red blood cells and the hemoglobin extracts had a much lower oxygen affinity. Thus, in this species, the O~2~ carrier is qualitatively (and, according to the previous report, quantitatively) polymorphic, and the polymorphism is reflected in respiratory properties as well as quaternary structure. The origin of the different hemoglobin phenotypes, however, is not yet clear. © 1993 Wiley‐Liss, Inc.