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Articles by Golam Sadik
Total Records ( 5 ) for Golam Sadik
  Maruf Ahmed , M. Helal Uddin Biswas , M. Motiur Rahman , M. Shah Alam Bhuiyan , M. Abu Hena Mostofa Kamal and Golam Sadik
  The study was conducted for the determination of Aspirin in blood sample by spectrophotometeric method. This is based on the formation of a color complex of the drug in serum with ferric-mercuric reagent. The absorbance of the colored complex was then measured at 540 nm for maximum absorption. This method shows linearity in the range of 0-100μg/ml and useful for the routine analysis of drug in the serum.
  Golam Sadik , Haideki Kozono , Kazuya Takeda , Parvez Hassan , Mir Imam Ibne Wahed and Tomotaka Shinoda
  Alzheimer`s amyloid βA4 protein fused with glutathione S-transferase (GST) was highly expressed using a strong prokaryotic expression system in Escherichia coli. The expressed protein had expected molecular mass on SDS-PAGE and appeared exclusively immunoreactive with antibody specific for βA4 epitope. This recombinant protein was purified with a combination of urea solubilization and ion exchange chromatography. To identify the human serum proteins which interact with βA4, affinity columns were prepared by immobilizing GST- βA4 and GST respectively. Using the affinity columns and human serum, we have observed an interaction of βA4 with serum proteins. Two proteins of Mr 45 and 15 kDa were identified on SDS-PAGE to be involved in the interaction. Our demonstration of the ability of βA4 to interact with serum protein strongly support the notion that such an interaction may underlie with the biological function of βA4 in vivo.
  Golam Sadik , Kazuya Takeda , Hiroyuki Kaji , Masato Taoka and Tomotaka Shinoda
  Amyloid βA4 peptide, the principal constituents of the senile plaques in Alzheimer`s disease (AD) originates from proteolysis of a larger protein precursor (APP). Several lines of evidence suggest that this peptide may be generated from aggregated precursor through nonspecific proteolysis. In this work, we used a sensitive in vitro method of detection to investigate the role of nonspecific proteases in the processing of a 100-amino acid C-terminal fragment (C100) inclusive of βA4 and cytoplasmic domain of APP. We demonstrate first that C100 forms high molecular weight aggregates in vitro as determined by size exclusion chromatography. Digestion of aggregated C100 with the nonspecific enzyme, proteinase K resulted in cleavage at the amyloidogenic -secretase sites. This occurred at Ala 42-Val 43 generating βA4 12-42 & βA4 16-42 amyloid peptides. The enzyme cleaved most of the peptide bonds of the cytoplasmic domain and the upstream of βA4 domain of the substrate. The result suggests that both the N- and C-terminus βA4 can be generated by nonspecific proteases, acting on a aggregated substrate and support the notion that the βA4 can be formed in organelles containing proteases capable of cleaving most peptide bonds.
  Farque Ahmed , Abu Sayeed , Anwarul Islam , S.M. Abdus Salam , Golam Sadik , M.A. Sattar and G.R.M. Astaq Mohal Khan
  The petroleum ether, ethyl acetate and methanol extracts of Vanda roxburghii as well as glycoside, melianin (VR-1) isolated from it were screened for antimicrobial activity against a wide variety of bacteria and fungi. The ethyl acetate and methanol extracts showed moderate antibacterial activity against almost all the tested organisms. The compound melianin (VR-1) exhibited strong activity against all the tested organisms and produced zone of inhibition between 17 and 27 mm. The petroleum ether extract was found comparatively less active against the organisms. All the tested materials showed antifungal activity against Aspergillus fumigatus, Candida albicans, Hensinela californica and Rhizopus arijae. The minimum inhibitory concentrations (MIC) of melianin against Bacillus cereus, Bacillus subtilis, Escherichia coli and Shigella dysenteriae were 32, 64, 64 & 128 μg ml–1 respectively. The findings may provide the basis for traditional use of this plant in the treatment of infectious diseases.
  Chand Sultana , M. Aziz Abdur Rahman , M.A.A. Al-Bari , M.L.A. Banu , M. Saidul Islam , N. A. Khatune and Golam Sadik
  Three cadmium coordination complexes (cadmium deprotonated phthalyl pyridine [Cd(DPH)(Py)2, C1], cadmium deprotonated phthalyl 8-hydroxy quinoline [Cd(DPH)-8-HQ, C2] & cadmium deprotonated phthalyl isoquinoline [Cd(DPH)IQ, C3] and two addition compounds 1:1 antimony(III) chloride with acetophenone [SbCl3.C6H5COCH3, C4] & 1:1 arsenic(III)bromide with benzamide [AsBr3.C6H5CONH2, C5] were tested for their antimicrobial activity by disc diffusion and serial dilution methods. All the compounds were active against various test pathogenic organisms. The maximum antibacterial and antifungal activities were shown by the compound C4. The minimum inhibitory concentration (MIC) of the compound C4 was determined against two Gram positive (Bacillus subtilis and Streptococcus ß-haemolyticus) and two Gram negative (Shilgella dysenteriae, Salmonella typhi) bacteria and the values were found between 4 and 16 μg ml-1.
 
 
 
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