Immunochemical cross-reactivity between cyanogen bromide fragments of human serum albumin

The antigenic structure of human albumin was investigated in order to establish whether or not there was any similarity between its antigenic sites. Using immunoadsorbent columns prepared with cyanogen bromide fragments of human serum albumin, antibodies directed against different portions of the albumin molecules were isolated. Measurement of the amount of the antibodies isolated and study of their specificity by inhibition techniques show that these subpopulations of antibodies reacted not only with the fragment used for their isolation (homologous) but also with the other fragments (heterologous). Heterologous fragments were inhibiting only at a very high concentration with regard to the homologous ones. These results show that there is a weak cross-reactivity between different portions of the albumin molecule. This reaction is most probably due to the homology existing in the sequence of the human albumin molecule which has arisen by gene duplication. The same type of behavior can be predicted to extent to other molecules which have evolved by similar mechanisms.     

The primary structure of histone H3 from the nematode Caenorhabditis elegans

The complete amino acid sequence of histone H3 (135 residues) from the nematode Caenorhabditis elegans has been established. Microheterogeneity occurs at positions 96 and 100 of the chain. The sequences of the nematode H3 isoforms are very similar to the major chain of calf thymus H3 with which they show 4 substitutions in total. The major variant has cysteine in position 96. This is the first report of cysteine in this position in H3 from non-mammalian tissue. An exceptional methylation site has been detected at position 79. Various other sites of secondary modification are of a conservative nature.     

A study of connective tissue macromolecules in skin of mice with goldthioglucose-induced obesity.

The effect of obesity on the connective tissue composition of skin was investigated in mice with goldthioglucose (GTG)-induced obesity. Four months after GTG treatment, the obese animals were sacrificed. Acid mucopolysaccharides, glycoproteins, collagen, and elastin were analyzed in the skin and compared to the controls. Total MPS in the skin from obese animals decreased, reflected mostly in hyaluronic acid. Chondroitin showed an increase over controls. The content of soluble glycoproteins varied; total carbohydrate and sialic acid of the glycoprotein tended to increase with obesity. Collagen and elastin both tended to decrease with obesity.