Abstract
The serial osmotic hemolysis procedure of Simon and Topper [18] has been applied to chicken erythrocytes. Some of the chickens had been injected with 59Fe at various times prior to bleeding, thus giving rise to labeled red cells of different ages. Others had not been injected but their blood was labeled with 51Cr in vitro. The osmotically lysed fractions were also analyzed for the enzyme activity levels of lactic acid dehydrogenase and glutamic-oxalacetic transaminase. It was found that: 1. 1. Chicken red blood cells, like mammalian erythrocytes, exhibit a correlation between age and resistance to hypotonic lysis. The serial osmotic hemolysis procedure differentiates two populations of young cells, one fragile and one resistant. While two such populations have been found in the mammalian system, the resistant young chicken cells are more fragile than the corresponding mammalian young cells. 2. 2. Determination of relative-specific enzyme activities (LDH and GOT) indicates that only a small, fragile young cell component (which is found in both mammals and chickens) is associated with increased enzyme activities but that the bulk of young chicken cells exhibits only average enzyme levels. These results indicate that the decline of enzymatic activity in the chicken red blood cell on maturation proceeds more rapidly than in the mammalian cell. 3. 3. The distribution of the 51Cr label among chicken erythrocytes, in contradistinction to the mammalian system, is independent of red blood cell age. Since the preferential chromium binding by young mammalian erythrocytes has been shown to be due to the preferential binding of chromium by the younger hemoglobin, it is probable that the chicken hemoglobin, which greatly differs structurally from mammalian hemoglobin, is either not structurally altered on aging or, at least, not in a way such as to affect the extent of chromium binding.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.