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Biomedical subjects

M Abdullah

Publications and source records attributed to M Abdullah.

At least 55 records · Page 3Linked to original sources
PubMed1986

Fetuin: a serum component associated with rat Sertoli and spermatogenic cells in coculture.

Cocultures of rat Sertoli-spermatogenic cells plated in a culture medium supplemented with 10% fetal bovine serum for 6-12 h and then maintained in serum free, hormone/growth factor-supplemented medium accumulated an acidic glycoprotein of molecular weight of 68,000 dalton (68 kD) and isoelectric point range of about 4.2-3.5. Anion exchange chromatography has allowed the partial purification of this protein, which consists of a major protein band of 68 kD and two minor, low molecular weight components. A rabbit antiserum raised against the 68 kD component also crossreacts with the two low molecular weight components, thus suggesting that these two minor components are antigenically related to the 68 kD protein. The 68 kD protein has been identified as fetuin, the major component of fetal bovine serum, based on similar molecular weight, isoelectric point, immunoreactivity and trypsin inhibitory activity. Labeling experiments with [14C]amino acid mixture show that 68 kD protein is not synthesized by cocultured rat Sertoli and spermatogenic cells. Immunocytochemistry and Western blot approaches carried out under various experimental conditions support the view that the fetuin-68 kD protein is taken up from serum by both Sertoli cells and pachytene spermatocytes. Because fetuin 1) behaves as a carrier protein for growth factors, 2) has protease inhibitory activity, 3) is preferentially internalized by Sertoli cells and pachytene spermatocytes and 4) fetal bovine serum-supplemented medium impairs spermatogenic cell viability, there is a need to further define appropriate conditions for optimizing long-term viability and differentiation of spermatogenic cells in vitro.

Amino Acids↗
PubMed1985

The application of DNA-cellulose chromatography in the isolation of immunoglobulin M and complement component C4b-binding protein from human serum.

By utilising the ability of some anionic serum proteins to bind to DNA-cellulose, at physiological pH and ionic strength, two such proteins have been purified and identified as immunoglobulin M (IgM) and complement component C4b-binding protein (C4BP). The method entails ammonium sulphate precipitation followed by QAE-Sephadex, DNA-cellulose and Sephacryl S-300 chromatographic steps. Fractionation of the anionic proteins eluting from QAE-Sephadex over a selected range of ionic strength has afforded IgM which was characterised electrophoretically and immunochemically. A mixture containing IgM complexed with C4BP has also been obtained by utilizing fractions eluted from QAE-Sephadex at higher ionic strength. C4BP can be isolated from this mixture by using immunoaffinity chromatography to remove IgM.

Carrier Proteins↗
PubMed1985

Seasonal variations, and the intra-household distribution of food in a Bangladeshi village.

Individual food intakes and body weights were measured in 53 rural Bangladeshi households at four seasons. Energy and protein intakes (kcal/kg/d) showed significant seasonal differences for adults and young children (1-4 yr). Energy intakes of women and children were expressed as a proportion of the male household heads', to give an indicator of food allocation. Women's and older children's proportional energy intakes remained constant through the year, and in line with expected values. Young children's proportional intakes were low, girls' being lower than boys'. The only seasonal variation was an increase in young girls' proportional energy intake when household food supplies were lowest. It is concluded that women's proportional intakes are not depressed when family food intake decreases. There is evidence that young girls receive particularly low intakes.

Adolescent↗
PubMed1983

The purification of alpha 1-antichymotrypsin from human serum using DNA-cellulose chromatography.

By exploiting its capacity for binding to DNA, the protease inhibitor alpha 1-antichymotrypsin has been isolated from human serum by ammonium sulfate fractionation and successive chromatography on QAE-Sephadex, DNA-cellulose, and Sephacryl S-300. This experimental procedure compares favorably with existing methods for preparing alpha 1-antichymotrypsin in terms of overall yield and practical convenience. The purified alpha 1-antichymotrypsin was homogeneous as judged by electrophoretic and immunoelectrophoretic criteria. From its inhibition of the fluorimetric titration of chymotrypsin with 4-methylumbelliferyl-p-trimethylammonium cinnamate it was shown to combine with chymotrypsin in a 1:1 molar ratio and thus to retain its biological activity.

Chemical Phenomena↗
PubMed1979

Study of food habits, food practices and taboos in Bangladesh: their implications in nutrition education.

The paper reports the findings of a retrospective study conducted to determine the prevailing food habits, food taboos and practices among 381 mothers selected randomly from twelve villages situated in 4 administrative divisions of Bangladesh. Undesirable food taboos and practices, maldistribution of food, lack of understanding of the nutritional needs of the vulnerable groups and bad cooking practices were found to be widespread in rural Bangladesh. Nutritional and health implications of these are discussed and remedial measures suggested.

Adult↗
PubMed1977

The action pattern of human salivary alpha-amylase in the vicinity of the branch points of amylopectin.

Salivary alpha-amylase hydrolyses amylopectin in stages. At the end of the so-called second stage, there are present glucose, maltose, and a series of alpha-limit dextrins containing (1 leads to 4)- and (1 leads to 6)-alpha-D-glucosidic bonds. The structures of the limit dextrins containing a single (1 leads to 6)-bond were examined. Six such dextrins were found. Of these, two were capable of being further hydrolysed by alpha-amylase, whereas the remaining four were true, amylase-resistant alpha-limit dextrins. The structures of the limit dextrins afforded information about those (1 leads to 4)-alpha-D-glucosidic bonds of amylopectin that are capable of being cleaved by salivary alpha-amylase and those that are resistant. In order to define further the action of alpha-amylase, the alpha-amylolytic products of 6-alpha-maltotriosyl-D-glucose, 6(3)-alpha-maltotriosylmaltotriose, and 6(3)-alpha-maltotriosylmaltotetraose were examined.

Amylases↗