MAMMALIAN HEMOGLOBINS 



313 



strains possess single hemoglobins that are electrophoretically similar in starch gels, 

 but three of these single hemoglobins have different solubilities in phosphate buffer 

 (figure 44) . The solubility of a 50/50 mixture of SeC and C57BL hemoglobins is inter- 

 mediate between that of SeC and C57BL. The quantity and form of crystals that 



Fig. 44. Comparison of murine carbonmonoxyhemoglobins analyzed by salting-out 



METHODS. 



0.72-1 

 0.64- 



f-0.56- 



0.48- 



UJ 



5 0.40 



n- 0.32 



o 



o 



* 024 



Ll. 

 O 



0.16- 



0.08- 



231 2.45 2.59 2.73 2.87 



MOLARITY OF K 2 HP0 4 -KH 2 P0 4 AT pH 6.65 



3.01 



Optical density of carbonmonoxyhemoglobin filtrates obtained in phosphate buffers of 

 variable molarities were read at 575 m\x; physical conditions were 0.3 per cent solution of 

 hemoglobin, 21 hours of incubation, pH 6.65, 30° C. 



develop in 21 hours at 30° C. in a 2.73 M phosphate buffer, pH 6.7, can also be used to 

 distinguish the C57BL, (G57BL x SeC)F l5 and SeC hemoglobins. Data are presented 

 in table 58 on the inheritance of solubility characteristics of the single hemoglobins 

 of strain C57BL and SeC mice. Previous studies 1017 indicated that the hemoglobin 

 locus that governs the molecular characteristics which determine the electrophoretic 

 behavior of single and diffuse hemoglobins is closely linked to the chinchilla locus of 

 linkage group I. Data in table 58 show that the chinchilla locus and the locus that 

 controls the molecular characteristics which determine the solubility properties of 

 C57BL and SeC hemoglobins segregate independently. Thus, at least two loci appear 

 to be involved in directing the physical and chemical characteristics of hemoglobins 

 in the mouse. Data on solubility, crystallography, and electrophoretic characteristics 



