PDF] Hemoglobin polymorphism in white-tailed deer: subunit basis

By A Mystery Man Writer

It was concluded from the results of limited structural studies that there were multiple peptide differences upon comparison of three non-α polypeptide chains in white-tailed deer. A variety of aberrant erythrocyte forms have been related to seven adult and two fetal hemoglobins in white-tailed deer. While sickling of the erythrocyte was not associated with a single hemoglobin type, it was precluded by hemoglobin V or VII, even when in combination with other hemoglobin types normally associated with sickling. The subunit basis of the hemoglobin polymorphism was presented. Two kinds of α subunits, six kinds of β subunits and one γ subunit were related to the whole hemoglobin molecule. The heterogeneity of the deer hemoglobins was based upon a variety of combinations of these numerous polypeptide chains. It was concluded from the results of limited structural studies that there were multiple peptide differences upon comparison of three non-α polypeptide chains.

Relaxed functional constraints on triplicate α-globin gene in the

Diversity, Free Full-Text

Ultrastructure of Sickled Deer Erythrocytes. I. The Typical

High-altitude deer mouse hypoxia-inducible factor-2α shows

A Structural Analysis of the FDA Green Book-Approved Veterinary

Lubert Stryer - Biochemistry.pdf

Alteration of the α1β2/α2β1 subunit interface contributes to the

(PDF) Pan-American Trypanosoma (Megatrypanum) trinaperronei n

Frontiers A New Homotetramer Hemoglobin in the Pulmonary

Multiplicity and Polymorphism of Fish Hemoglobins

©2016-2024, slotxogame24hr.com, Inc. or its affiliates