Isolation and Characterization of Recombinant Variable Domain of Heavy Chain Anti-idiotypic Antibodies Specific to Aflatoxin B_1

Some unique subclasses of Camelidae antibodies are devoid of the light chain, and the antigen binding site is comprised exclusively of the variable domain of the heavy chain （VHH）. The recombinant VHHs have a high potential as alternative reagents for the next generation of immunoassay. In particular, they might be very useful for molecular mimicry. The present study demonstrated an alpaca immunized with the F（ab＇）z fragment of anti-aflatoxin B1 mAb and developed an important anti-idiotypic （anti-ld） responses. Antigen-specific elution method was used for panning private anti-ld VHHs from the constructed alpaca VHH library. The selected VHHs were expressed, renatured, purified, and then identified by a competitive enzyme-linked immunosorbent assay （ELISA）. Our findings indicated that the VHH would be an alternative tool for haptens mimicry studies.

Isolation and Characterization of the Cytoplasmic Male Sterility Associated Gene of Cotton(Gossypium harknessii)

Cytoplasmic male sterility(CMS) is a maternally inherited trait that results in the failure to produce functional pollen.It was identified in many plants,and it is widely used to exploit heterosis.

The isolation and characterization of indole alkaloids from the fruits of Kopsia officinalis

Sixteen alkaloids have been isolated from the fruits of Kopsia officinalis Tsiang and P.T. Li(Apocynaceae), a plant commonly used in folk medicine for treating tonsillitis and rheumatism. Ten of them were identified as known alkaloids-eburnamenine(1), kopsanone(2), 5, 18-dioxokopsan (3), kopsinilam(4), kopsinine(5), pleiocarpine(6), kopsamine(7), N-carbomethoxy-12-methoxykop- sinaline(8), N-carbomethoxy-11, 12-dimethoxykopsinaline (9) and(+)-vincadifformine (13). The other three have now been proved to be new. They are N-carbomethoxy-11-hydroxy-12-methoxy- kopsinaline(10), N-carbomethoxy-11-methoxy-12-hydroxykopsinanne (11) and kopsamine N-oxide (12).

Characterization and phylogenetics of a new species of genus Lactobacillus from the activated sludge in biohydrogen production

Anaerobic process of biohydrogen production was developed. There is a great deal of Lactobacillus bacteria in the activated sludge of biohydrogen reactor. The isolation and identification of different anaerobic bacteria in the reactor is important for fermented biohydrogen production process by anaerobic digesting organic wastewater. Considering with the physiological and biochemical traits,morphological characteristics and 16SrDNA sequence,the isolated Rennanqilyf13 is a new species in Lactobacillus genus. And the temporary nomenclature of the species is Lactobacillus Strain Rennanqilyf13 sp. nov.

Identification of a marine agarolytic bacterium Agarivorans albus QM38 and cloning and sequencing its beta-agarase genes

A total of 117 agar-decomposing cultures were isolated from coastal seawater around Qingdao, China. The phenotypic and agarolytic features of an agarolytic isolate, QM38, were investigated. The strain was gram negative, strictly aerobic, curved rod and polar flagellum. On the basis of several phenotypic characters, biochemical and morphological characters and phylogenetic analysis of the gene coding for the 16S rRNA, the strain was identified as Agarivorans albus strain QM38. This strain can liquefy the agar on the solid agar plate. An excellular agarase activity was determined in liquid culture. The enzyme exhibited maximal activity at 40 ℃, pH 7.6. Its activity was greatly affected by different concentrations of agarose. The highest activity 32 U/ml was achieved in the culture supernatant. The hydrolytic product was analyzed by fluorophore-assisted carbohydrate electrophoresis （FACE）. After complete hydrolysis of agarose, a series of agaro-oligosaccharides were produced. The main products of the enzymes were oligosaccharides in the degree of polymerization （DP） of 2, 4, 6 and 8. Three genes agaD01, agaD02 and agaD03, encodingβ-agarases, had been cloned from genomic DNA of Agarivorans albus strain QM38. The open reading frame of agaDOl, consisted of 2 988 bp, and shared 95.5%-98.9% identity to the β-agarase genes of some strains of Vibrio and Agarivorans. Gene agaD02 comprised 2 868 bp and encoded a 955- amino-acid protein. It showed 97.4% and 98.7~0 identity to the β-agarase genes of strain Vibrio sp. PO-303 and strain Vibrio sp. JT0107, respectively. Only partial sequence of agaD03 gene has been cloned. It showed 96.5% identity to β-agarase gene （agaB） of Pseudoalteromonas sp. CY24, and shared 96.8% identity to β-agarase-c gene of Vibrio sp. PO-303.