Amino acid compositions of the tryptic peptides comprising the β‐hemoglobin chain of Macaca nemestrina

The tryptic peptides comprising the aminoethylated β‐hemoglobin chain of Macaca nemestrina were isolated by paper electrophoresis and chromatography. The results of stains for specific amino acids, comparison of peptide maps with those produced by aminoethlated β chains from human hemoglobin A, and amino acid analyses of all peptides in the macaque β chain support the conclusion that the primary structure of the β chain of M. nemestrina is identical to that of the corresponding chains of M. fuscata fuscata and M. fascicularis. The apparent evolutionary conservatism of macaque β chains is discussed in relation to the wide degree of structural variation previously observed among the α‐hemoglobin chains of several species of Macaca. Copyright © 1974 Wiley‐Liss, Inc., A Wiley Compan

Multiple fetal and adult hemoglobins in Malaysian Macaca nemestrina: Consequences of a‐chain variation

The hemoglobins of fetal and adult Macaca nemestrina were investigated electrophoretically and chromatographically. Standard electrophoretic techniques failed to reveal variation in either fetal or adult hemoglobins beyond that previously attributed to the presence of the duplicate γ‐chain loci characteristic of this species. However, column chromatography of whole hemolysates on CM‐Sephadex or of globin chains on CM‐cellulose in 8 M urea revealed that some fetuses had four major hemoglobins and some adults had two major hemoglobin components. All animals examined were of Malaysian origin; the variation described is a consequence of variation in α‐chain structure in Malaysian populations of this species, and of the interaction of different α chains with the products of the duplicate γ‐chain loci. Copyright © 1974 Wiley‐Liss, Inc., A Wiley Compan

Differential effect of chloramphenicol and actinomycin D on protein synthesis in the decapod crustacean upogebia littoralis

Chloramphenicol and actinomycin D produced opposite effects on the in vivo protein synthesis by the hepatopancreas of the crustacean Upogebia littoralis. Inhibition of protein synthesis was noted within 6 hours after administration of chloramphenicol; maximum inhibition occurred 8 hours after treatment. No inhibition was noted after administration of actinomycin D; on the contrary, this antibiotic appeared to slightly stimulate protein synthesis as measured by rate of C14-leucine incorporation, within 6 to 8 hours after treatment. © 1972 Dr. W. Junk n.v. Publishers