Raymond A. Popp, Ph.D. 



MAMMALIAN HEMOGLOBINS t 



Variability among mammalian hemoglobins was recognized many years 

 ago, 33 ' 51 - 285 ' 732 ' 1047 but recent advances in methods for their identification, separa- 

 tion, and more complete characterization have enabled biologists to utilize differences 

 between hemoglobin to probe more deeply into the challenging and tantalizing prob- 

 lem of the mechanisms of genie function. Physical methods for distinguishing mam- 

 malian hemoglobins have been the subject of many papers since 1940. Technologic 

 advances in protein chemistry are now being applied to analyze the chemistry of 

 hemoglobins as well as other molecules of biological importance. Chemical analyses 

 of the content and sequence of amino acids in some peptide chains have been reported 

 for a variety of mammalian hemoglobins within recent years. The chief objective 

 of this review is to cite methods that have been applied in studies of mammalian 

 hemoglobins and to compare and evaluate the usefulness of each method for survey, 

 preparative, and/or analytical procedures. 



GENERAL COMMENTS 



Attempts to elucidate the nature of genie action have been based on the premise 

 that the specific physical and chemical properties of macromolecules are reflections 

 of the function and specificity of genes. The molecules chosen for such studies should, 

 as far as can be determined, be primary products of genie action, have similar biological 

 functions and similar physical and chemical properties, yet occur as intra- or interspecies 



f Some of the analyses in this paper were made possible through the cooperation of 

 Dr. Norman G. Anderson and his group. 



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