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INDONESIA
ANNALES BOGORIENSES
Published by Lembaga Ilmu Pengetahuan Indonesia
ISSN : 05178452     EISSN : 24077518     DOI : -
Core Subject : Health, Science, Agriculture, Engineering,
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Immunology & microbiology Medicine & Pharmacology
The Annales Bogorienses (ISSN: 0517-8452, E-ISSN: 2407-7518) is a peer-reviewed Journal that is published biannually. First published in 1955, it is now one of the oldest scientific journal in the nation. The Annales Bogorienses publishes original articles in basic and applied research as well as critical reviews and short communication in the fields of life sciences with the emphasis in biotechnology, molecular biology, and biochemistry.
Arjuna Subject : -
Articles 540 Documents
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Front Cover AB Vol 17 No 1 (2013) Lisdiyanti, Puspita
ANNALES BOGORIENSES Vol 17, No 1 (2013): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.1234/169

Abstract

Detection of Potyvirus using RT-PCR and ACP-ELISA of Dioscorea species and in vitro shoot multiplication of the virus free plants Wulandari, Dyah Retno; Ermayanti, Tri Muji
ANNALES BOGORIENSES Vol 15, No 2 (2011): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (273.445 KB) | DOI: 10.1234/41

Abstract

Detection of Potyvirus using Reverse Transcription-Polymerase Chain Reaction (RT-PCR) and Antigen Coated Plate-Enzyme Linked Immunoabsorbent Assay (ACP-ELISA) for Dioscorea alata, D. hispida and D. esculenta was conducted in order to establish in vitro culture of virus-free of these species. Plants were collected from Yogyakarta, Lampung, Pasuruan, Jakarta and Bogor. Total RNA of plants grown in a greenhouse was then isolated according to Simple Direct Tube (SDT) method. Total RNA from symptomatic leaf of Yard Long Bean (Vigna unguiculata) infected with Bean Common Mosaic Potyvirus (BCMV) was used as the positive control treatment. RT-PCR assay with degenerate primers MJ1(F) and MJ2(R) was used to identify the Potyviruses infecting Dioscorea. ACP-ELISA with antibodies specific to group Potyvirus was carried out to detect Potyvirus from leaves samples. The Dioscorea virus-free species was then cultured on modified MS medium. Shoot tips or internodes were used as explants. The results showed that using both RT-PCR and ACP-ELISA, all species tested were free from virus. The growth response of explants on MS medium was varied depending on the plant species and the concentration of BAP.   Keywords: Dioscorea spp., Potyvirus, RT-PCR, ACP-ELISA, in vitro shoot multiplication
Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in Escherichia coli Dewi, Kartika Sari; Fuad, Asrul Muhamad
ANNALES BOGORIENSES Vol 21, No 1 (2017): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (450.568 KB) | DOI: 10.14203/ab.v21i1.299

Abstract

Several studies reported that the expression of various kinds of Single-chain variable fragment (scFv) antibodies in Escherichia coli are significantly influenced by the order of their variable domains. To date, the effect of the order of variable domains in the expression of scFv antibodies against epidermal growth factor receptor variant III (EGFRvIII) has not been reported. This study aimed to compare the expression between VH-linker-VL and VL-linker-VH domain orders of the anti-EGFRvIII scFv antibodies in E. coli expression system. Recombinant plasmids inserted with DNA encoding scFv proteins were transformed into E. coli NiCo21(DE3) competent cells and characterized by colony PCR. The expression of scFv proteins was done by using optimum concentration of inducer. Total proteins, soluble periplasmic and cytoplasmic proteins, also extracellular proteins were isolated, subsequently characterized by SDS-PAGE, Slot Blot, and ImageJ software analyses. The antigen-binding activity of both scFvs proteins against EGFRvIII was observed. The results showed that the relative percentage of scFv expression with VH-linker-VL domain order is higher than that of VL-linker-VH in each compartment. Moreover, both of scFvs proteins have antigen-binding activity against EGFRvIII.
Editors Preface AB Vol 19 No 1 (2015) Dzikri, Muhamad
ANNALES BOGORIENSES Vol 19, No 1 (2015): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (309.806 KB) | DOI: 10.14203/ab.v19i1.267

Abstract

Role of Lactobacillus helveticus on Flavor Formation in Cheese: Amino Acid Metabolism Widyastuti, Yantyati; Lisdiyanti, Puspita; Tisnadjaja, Djadjat
ANNALES BOGORIENSES Vol 18, No 1 (2014): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.1234/88

Abstract

Lactic acid bacteria, mainly lactobacilli, play an important role in cheese making. Their role can be divided into starters and non-starters or secondary microorganisms. Lactobacillus helveticus, an obligatelyhomofermenter and thermophilic bacterium, has unique properties as a starter because of its ability to inducestrong impact on cheese flavor. The bacteria are known to be prototrophic for 5 amino acids and auxotrophic for 13 amino acids. It is interesting that the conversion of aromatic amino acids, branch chain amino acids, and methionine into volatile and nonvolatile compounds by L. helveticus is thought to represent the rate-limiting step in the formation of mature flavor and aroma in cheese. The addition of a highly autolytic L. helveticus to a starter system could significantly increase the formation of flavor precursor and some volatile compounds during cheese ripening. This article focuses on the contribution of L. helveticus to flavour compound formation in cheese with particular emphasis on amino acid metabolism.
Agrobacterium-mediated transformation of banana Musa acuminata AA cv "“Mas Lampung” with hpt gene using sterile corm as target tissue Nena, Ade; Witjaksono, Witjaksono; Estiati, Amy
ANNALES BOGORIENSES Vol 13, No 1 (2009): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (285.979 KB) | DOI: 10.1234/27

Abstract

The protocol for  Agrobacterium-mediated transformation of local banana plants cv  “Mas Lampung” (AA) has been established. A selectable marker gene (hpt) has been used to study the transformation using  in vitro corm slices as target tissues.  Banana  in vitro corm slices were co-cultivated with the EHA105 strain of Agrobacterium tumefaciens harbouring binary vector pCAMBIA 1301 containing hygromycin resistance gene (hpt) as a selectable marker and intron-containing β-Glucuronidase (gus-intron) gene as a reporter gene driven by  CaMV 35S promoter.   Polymerase Chain Reaction (PCR) were used to examine the existence of  hpt gene in plants resulted from the transformation.  Using primer pairs specific for hpt gene, our PCR analysis on leaves showed the presence of the  hpt   transgene in banana transgenic plants at first generation (T0) of transformation.  To prove the existence of hpt gene in the fruits of transgenic banana plants, PCR analysis were also carried out.  The data showed that the  hpt  gene could be amplified  from banana fruits of tested samples.   These result demonstrates that the Agrobacterium-mediated transformation method used in this experiment has been successful to transfer gene into banana plants. Thus, the transformation method reported here could be used as a standard protocol to  transfer another useful genes into local banana plants cv. “Mas Lampung”.  Furthermore, the presence of transgene in fruits of banana transgenic plants is important achievement  especially for transgene that is expected to be expressed in the fruit including to introduce vaccine genes into banana fruits for edible vaccine.Key words:  Agrobacterium,  hpt  gene, transgenic banana Mas Lampung, Musa acuminate corm slices, PCR
Constitutive Expression of Candida antarctica Lipase B (CALB) in Pichia pastoris Using pGAPZα Vector Wahyuni, Febriana Dwi; Fuad, Asrul Muhamad; Suharsono, Suharsono
ANNALES BOGORIENSES Vol 20, No 1 (2016): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (461.586 KB) | DOI: 10.14203/ab.v20i1.225

Abstract

The CalBsyn gene was previously constructed synthetically to encode Candida antarctica lipase B (CALB). Lipase from CalBsyn gene is slightly different from that of wild type CALB (CALB-wt) where it has three amino acids substitutions at different positions, i.e. V210I, A281E, and V221D, to improve enzyme’s thermostability and catalytic efficiency. The CalBsyn gene was isolated from pJ912-CalBsyn vector by digestion using XhoI restriction enzyme. The CalBsyn gene then was ligated to pGAPZα expression vector and transformed into E. coli TOP10F’ in order to obtain recombinant vector pGAPZα-CalBsyn. The result showed that pGAPZα-CalBsyn recombinant vector was successfully transformed into E. coli TOP10F’ with transformation efficiency of 4.11 x 103 cfu/µg plasmid DNA. The pGAPZα-CalBsyn recombinant plasmid was successfully introduced into Pichia pastoris SMD1168H using electroporation method with transformation efficiency of 1.01 x 102 cfu/µg DNA. Qualitative lipase activity assays showed that transformed P. pastoris secreted recombinant lipase (CALB) and has lipolytic activity; while quantitative lipase activity assays showed that the lipase activity was 63.5 Units/ml in 48 hours. Analysis using SDS-PAGE showed that CALB protein was expressed successfully and the recombinant protein’s molecular size was approximately 45 kDa.
Identification of Cadalene-β-Carboxylic Acid from Barks of Bawang Hutan (Scorodocarpus borneensis Becc.) Kartika, Rudi; Bustanussalam, Bustanussalam; Simanjuntak, Partomuan
ANNALES BOGORIENSES Vol 16, No 2 (2012): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1847.255 KB) | DOI: 10.1234/66

Abstract

One sesquiterpene compound has been isolated and identified out of the ethylacetate extract of bawang hutan (Scorodocarpus borneensis Becc.) barks. The barks were macerated with methanol, and then partitioned with mixture of ethylacetate-water (1:1).  Fractionation of the ethylacetate phase by column chromatography gave pure compound. Based on data interpretation from of ultra-violet (UV) spectra, Fourier Transform Infra Red (FT-IR), NMR 1D (1H and13C-NMR); NMR 2D (HMQC, COSY, HMBC), and comparison with literature, the pure isolated compound was determined as sesquiterpene   compound, cadalene-β-carboxylic acid, which exhibited LC50 of 42.32 ppm. Keywords: bawang hutan, Scorodocarpus borneensis, Olaceaeae, brine shrimp lethality test.
Subcloning, Expression and Characterisation of A Recombinant Antibody Fab-Fragment Specific Towards 2,4-D Kusharyoto, Wien
ANNALES BOGORIENSES Vol 10, No 1 (2005): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3633.744 KB) | DOI: 10.1234/15

Abstract

A generic strategy was established for subcloning the VH and VL gene of antibody variable domains into the plasmid pASK85 for the expression of Fab antibody fragments. pASK85 bears coding sequences for murine constant domains including a His6-tag at the carboxy-terminal end of the constant heavy-chain domain. The VH and YL gene derived from the monoclonal antibody E2/B5 specific towards 2,4-dichloropbcnoxyacetic acid (2,4- D) were used in this study. Eschericia coli was used as host cells for the biosynthesis of the Fab-fragment. The Fab­ fragment wa subsequently purified from the periplasmic extract in a single step by immobilised metal-ion affinity chromatography (IMAC). The production level obtained were 0.5-0.8 mg purified Fab-fragments per liter E. coli culture. The sensitivity and cross-reactivity of the Fab-fragment determined by direct competitive ELISA were similar to those of the parental monoclonal antibody E2/B5 .  
Sequential Adaptation in Mammalian CHO-K1 Cells Producing Human Erythropoietin Wisnuwardhani, Popi Hadi; Septisetyani, Endah Puji; Santoso, Adi
ANNALES BOGORIENSES Vol 21, No 1 (2017): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (289.139 KB) | DOI: 10.14203/ab.v21i1.282

Abstract

The production of recombinant proteins for clinical applications using mammalian cell technology has become a prevalent system because of its capacity in assembling functional proteins.  One of the main problems with CHO-K1 cells is that this cell has to grow in the presence of serum. However, the presence of serum will complicate the downstream step for protein production. Thus, protein produced in media without serum, theoretically, would be easier to purify.  Technically, this type of cell can be produced by growing the CHO-K1 cells in serum-free media by using adaptation method in suspension condition. This research showed that through sequential adaptation using conditioned media, the CHO-K1 cell line that produces the human erythropoietin gene (hEPO) was able to grow in suspension culture using serum-free media.  Based on Western blot analysis, it showed that the protein (hEPO) was able to be expressed in suspension culture with molecular mass of about 47 kDa.

Page 12 of 54 | Total Record : 540

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