Adenine induced granulocytosis in the rabbit.

Peripheral blood specimens from rabbits injected parenterally with physiological saline, adenine sulfate and guanine sulfate were examined for white blood cell count changes. A significant leukocytosis occurred within forty-eight hours only after adenine sulfate administration. A differential analysis revealed the increase was in the heterophil (pseudoeosinophil, amphophil) population. A mild lymphopenia was noted. There were no clear cut trends in the eosinophil, basophil and monocyte populations. No leukocyte morphological changes were found on peripheral blood smears.     

The cell-surface distribution of alloantigens on the bovine erythrocyte

The topographical distribution of genetically defined alloantigens of the bovine erythrocyte was investigated by a serological absorption procedure known as the blocking test. Blocking was observed between the E′₁ and Y₂ antigens in theB system when these occurred in the same phenogroup. E′₁ was also blocked by G and Q′ in the same phenogroup and Y₂ was blocked by G. No blocking was observed between specificities residing either in different phenogroups or in different systems. We conclude that the several specificities in a givenB-system phenogroup are carried on a single molecule having multiple antigenic determinants, and that this arrangement is entirely consistent with the hypothesis that these factors are controlled by multiple alleles at a single locus.     

OCCURRENCE OF N-ACETYL-l-GLUTAMIC ACID IN THE HUMAN BRAIN

A substance apparently identical with N-acetyl-l -glutamic acid was isolated from an aqueous extract from human brain by a combination of paper and ion exchange chromatography. The isolated substance does not react with ninhydrin reagent but yields glutamic acid upon acid hydrolysis. Acetyl hydrazide was identified by paper chromatography of hydrazinolysates of the isolated substance and N-acetyl-l -glutamic acid. The configuration was determined with l -specific hog kidney acylase.     

Human serum albumin adsorption onto a-SiC:H and a-C:H thin films deposited by plasma enhanced chemical vapor deposition

In the present paper, we report the study of the adsorption behavior of a model protein such as human serum albumin (HSA) onto surfaces of a-SiC:H and a-C:H thin films deposited by using the plasma-enhanced chemical vapor deposition (PECVD) technique. The surface composition and surface energy of the various substrates as well as the evaluation of the adsorbed amount of protein has been carried out by means of X-ray photoelectron spectroscopy (XPS) and contact angle measurements. It has been found that HSA tends to preferentially adsorb on Si-rich surfaces, as far as the relative amount of adsorbed HSA decreases with increasing S-C concentration. Preliminary elements of mechanistic models are proposed for the correlation between chemical factors and the observed protein adsorption behavior.     

Isolation of N-acetylglutamine, pyroglutamic acid and the butyl ester of pyroglutamic acid from human brain

N-acetyl-l -glutamine, pyroglutamic acid, and the butyl ester of pyroglutamic acid were isolated in pure form from an aqueous extract of human brain. These compounds were isolated by combination of paper and ion exchange chromatography. The isolated substance identified as N-acetyl-l -glutamine did not react with the ninhydrin reagent but yielded glutamic acid and ammonia upon acid hydrolysis. An acetyl hydrazide was identified by paper chromatography from hydrazinolysates of the isolated substance. The glutamic acid liberated by hydrolysis had the l -configuration. The results of elementary analysis of the isolated compound were in full accord with the analysis calculated for synthetic N-acetyl-l -glutamine. A large amount of pyroglutamic acid and a substance identical with the butyl ester of pyroglutamic acid were isolated in pure form. The results of our studies suggest that pyroglutamic and the butyl ester derivative were artifacts formed during the isolation and purification procedures.     

OCCURRENCE OF N-ACETYLALANINE IN THE HUMAN BRAIN1

A substance identical with N-acetyl-l -alanine was isolated from an aqueous extract of human brain by a combination of paper and ion-exchange Chromatography. The isolated substance did not react with ninhydrin reagent but yielded alanine upon acid hydrolysis. An acetyl hydrazide was identified by paper chromatography of hydrazinolysates of the isolated substance and N-acetyl-l -alanine. The unknown alanine had the l -configuration. The results of elementary analysis of the isolated compound were in full accord with the analysis calculated for synthetic N-acetyl-l -alanine.