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INDONESIA
Indonesian Journal of Biotechnology
Published by Universitas Gadjah Mada
ISSN : 08538654     EISSN : 20892241     DOI : -
Core Subject : Science,
Biochemistry, Genetics & Molecular Biology Immunology & microbiology Materials Science & Nanotechnology
The Indonesian Journal of Biotechnology (IJBiotech) is an open access, peer-reviewed, multidisciplinary journal dedicated to the publication of novel research in all aspects of biotechnology, with particular attention paid to the exploration and development of natural products derived from tropical—and especially Indonesian—biodiversity. IJBiotech is published biannually and accepts original research articles featuring well-designed studies with clearly analyzed and logically interpreted results. A strong preference is given to research that has the potential to make significant contributions to both the field of biotechnology and society in general.
Arjuna Subject : -
Articles 12 Documents
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Search results for , issue "Vol 13, No 1 (2008)" : 12 Documents clear
Epitope Mapping of Fc gamma RIIa Monoclonal Antibodies Caroline Tan Sardjono; Bruce Wines; Maree Powel; Mark Hogarth
Indonesian Journal of Biotechnology Vol 13, No 1 (2008)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (305.935 KB) | DOI: 10.22146/ijbiotech.7792

Abstract

FcγRIIa (CD32) is an IgG receptor which has been shown to be important in autoimmune disease pathology. IV.3, 8.7, and 7.30 are anti-FcγRIIa monoclonal antibodies (mAbs), which block the interaction between FcγRIIa and complex IgG. In this study, the three mAbs were demonstrated to inhibit FcγRIIa function. The determination of the precise epitopes of the IV.3, 8.7, and 7.30 mAbs may become a potential approach for designing inhibitors for FcγRIIa. The epitope of IV.3, 8.7, and 7.30 were determined using chimeric receptors based on the extracellular domains of FcγRIIa and the FcεRI a chain. The epitopes for IV.3 was found to be mapped on amino acid residues 132-137, while 8.7 and 7.30 were on amino acid residues 112-119 and 157-162. Based on the crystal 3D model of FcγRIIa molecule, these amino acid sequences are clustered together forming a contiguous region within the ligand binding site of the receptor.
PGV-1 is a Potent Antimitotic Agent Barinta Widaryanti; Muhammad Da’i; Masashi Kawaichi
Indonesian Journal of Biotechnology Vol 13, No 1 (2008)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (61.837 KB) | DOI: 10.22146/ijbiotech.7796

Abstract

Carcinogenesis may resulted from the malfunctioning of programmed cell death. Most of the anticancer drugs incurrent use induce apoptosis in susceptible cells. The fact that disparate agent interacting with different targets seemto induce cell death through some common mechanisms suggest that anticancer activity is determined by the abilityof inhibiting cell growth. Pentagamavunon-1 (PGV-1) is one of the curcumin analogues which showed to havepotency in inhibiting proliferation of T47D human breast carcinoma cells. The effects on T47D cells growth isassociated with cell cycle arrest in G2/M phase at the concentration of 2.5 ?M, followed by hyperploidy. The data onpolymerization assay, indicated that PGV-1 interact with tubulin in different manner from taxol. PGV-1 inhibittubulin polymerization on cell culture while taxol stabilized tubulin polymerization. Immunostainning data onPGV-1 treated cells showed slightly tubulin condensation, while taxol treated cells showed tubulin condensationdistinctly at 12 minutes after releasing from depolymerizing agent.In conclusion, PGV-1 represent a new microtubule inhibitor and has the potential to be developed for antimitoticdrugKey words: Pentagamavunon-1, T47D, tubulin

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