Search PubMed⌕ Search

Biomedical subjects

Z Malik

Publications and source records attributed to Z Malik.

116 records · Page 7Linked to original sources
PubMed1979

Effect of hemin and Protoporphyrin IX on the protein-synthesizing activity of human granulocytes, lymphocytes and platelets.

The hemin effect on protein synthesis of human granulocytes, lymphocytes and platelets was examined. Hemin added to culture media without serum caused a dose-dependent inhibition of protein synthesis in all three cell types. A cell-specific enhancement of protein-synthesizing capability was observed in 24-hour cultures in the presence of hemin and serum. A marked increase of protein synthesis was found in granulocytes, unchanged in lymphocytes and decreased in platelets. Lymphocytes from patients with chronic lymphatic leukemia (CLL) were moderately inhibited by hemin when incubated in media containing serum, the effect being more pronounced in the presence of freshly disolved doses of hemin. Addition of protoporphyrin IX to cells cultures resulted in a marked suppression of protein synthesis by the three cell types, in all experiments. These results confirm the importance of serum proteins in preventing the inhibitory effects of free hemin and protoporphyrin IX on blood cell protein synthesis. On the other hand, they show a cell-specific enhancement of the protein-synthesizing capacity mediated by hemin.

Blood Platelets↗
PubMed1979

Glycosylation of mouse embryonic hemoglobins in cultured yolk sac erythroblasts.

Embryonic hemoglobins of yolk sac nucleated erythroblasts were glycosylated in vitro by (3H)-glucose and the rate of glycosylation was maximal within 24 h of incubation. Isoelectric focusing of the glycosylated products revealed that both EI and EII embryonic hemoglobins have glycosylated components, EIg, EIIg, with pI very close to the native hemoglobins.

Animals↗
PubMed1979

The role of hemin in the regulation of heme synthesis by fetal mouse liver erythroblasts in culture.

The regulatory role of exogenous hemin on the heme synthetic pathway was studied in fetal mouse liver erythroblasts in culture. Hemin added to culture medium of 13th day embryo liver cells inhibited, dose dependently, the incorporation of the porphyrin precursors, 59Fe, 14C-2-glycine and 14C-5-aminolevulinic acid (ALA) by 85%, 70% and 45%, respectively. This suggests a multiple effect of hemin on the porphyrin biosynthetic enzymes. Exogenous ALA competed with 14 C-2-glycine as a porphyrin precursor, but the rate of heme synthesis, measured by 59Fe incorporation, remained unaltered. Protoporphyrin mimicked the hemin effect on the inhibition of glycine incorporation into heme, but reduced iron incorporation by only 20%. Erythroblasts, with an inhibited porphyrin biosynthesis, utilized exogenous 59Fe-hemin for hemoglobin assembly and maintained an undecreased level of hemoglobin synthesis. The results indicate that hemin inhibits the porphyrin biosynthesis in fetal mouse liver erythroblasts mainly at the iron incorporation stage.

Aminolevulinic Acid↗
PubMed1970

Antigenicity of proteinases from Streptomyces griseus (pronase).

The five pronase fractions, A(1), A(2), B, C (trypsin-like), and D (elastolytic), obtained by ion-exchange chromatography, were found to be antigenically distinct. Antibodies to pronase inhibited the enzymic activity of each of the enzyme fractions. Pronase trypsin and bovine trypsin, although resembling each other in enzymic activity and in amino acid sequence around their active sites, did not cross-react antigenically with, nor was their enzymic activity inhibited by, the respective homologous antibodies. Inactivation of pronase trypsin by complexing with soya-bean inhibitor AA, was not associated with a decrease in capacity to precipitate with its antibody. It is assumed that the antigenic sites are located far enough from the catalytic site of the enzyme to allow it to precipitate immunologically even when the catalytic site was blocked.

Amino Acid Sequence↗
PubMedDate not supplied

Separation of normozoospermic human spermatozoa into subpopulations by selective agglutination with peanut agglutinin.

Incubation of human spermatozoa of normozoospermic origin with the galactose specific lectin peanut agglutinin (PNA) resulted in agglutination of the majority of sperm. This finding enabled separation of sperm into two subpopulations. The major one, accounting for 87.0 +/- 12.7 (SD)% consisted of agglutinating sperm (PNA+), while the minor subpopulation (PNA-) did not bind the lectin. The correlation between the percentages of PNA- sperm and acrosome-damaged sperm, as detected by light microscopy prior to separation, was analysed and an overlapping has been found. Light and electron microscopy examination revealed that the PNA- cells were either acrosomeless or possessed severely damaged acrosomes while the PNA+ sperm were mostly free of such pathologies. Following treatment of sperm with fluorescin-conjugated PNA the single cells lacked any labeling while the agglutinates exhibited fluorescence. However, the binding of the lectin to sperm was non-uniform and differences in fluorescence intensity at various parts of the head have been observed. The sialic acid content in PNA+ sperm was found to be significantly higher (7.5 +/- 2.2 micrograms/10(8) sperm) as compared to PNA- sperm (2.1 +/- 0.6 micrograms/10(8) sperm). It was suggested that sialic acid content could be a biochemical indicator of acrosomal integrity. Separation of sperm by selective PNA agglutination might be valuable for elimination of sperm affected by acrosomal pathologies from the ejaculate.

Galactose↗
PubMedDate not supplied

A high proportion of double-headed and double-tailed sperm in semen of a human male. A case report.

We present the case of a patient whose semen contained 30% of sperm with double heads and double tails at various stages of attachment due to abnormal meiosis. The genital system, sperm density, endocrinological profile and karyotype were normal. It is postulated that abundance of the above-noted type of sperm pathology in the human semen might not necessarily be associated with oligozoospermia or fertility impairment.

Adult↗