Objective To evaluate the antigenic specificity of the enolase.Methods and Results The results included:(1)Western blot analysis demonstrated that enolase was a main protein in the nonglyco-proteins of C.albicans which could react with the serum of C.albicans infected rabbit.(2)The purified enolase was used to immunize rabbit for producing anti-enolase serum,and the hig hest titer of polyclonal antibody against enolase was up to 1:6400with enzyme-linked immunoadso rbent assay(ELISA).(3)Compared with three other polyclonal antibodies,anti-enola se antibody showed high specificity in detecting C.albicans antigen.Conclusion Enolase as a specific antigen,is worthy of further investigation in C.albicans cell.

0.05).No significant histological and ultrastructural changes were observed in the skin biopsies.Conclusion The long pulsewidth Diode Laser is a safe hair removal technique with good result and without adverse effect on the function of axillary sweat gland excretion.

Cold-adapted lipases are attractive biocatalysts that can be used at low temperatures as additives in food products, laundry detergents, and the organic synthesis of chiral intermediates. Cold-adapted lipases are normally found in microorganisms that survive at low temperatures. A fungi strain XMZ-9 exhibiting lipolytic activity was isolated from the soil of glaciers in Xinjiang by the screening plates using 1% tributyrin as the substrate and Victoria blue as an indicator. Based on morphological characteristics and phylogenetic comparisons of its 18S rDNA, the strain was identified as Penicillium sp. The partial nucleotide sequences of these two lipase related genes, LipA and LipB, were obtained by touchdown PCR using the degenerate primers designed according to the conservative domains of lipase. The full-length sequences of two genes were obtained by genome walking. The gene lipA contained 1 014 nucleotides, without any intron, comprising one open reading frame encoding a polypeptide of 337 amino acids. The gene lipB comprised two introns (61 bp and 49 bp) and a coding region sequence of 1 122 bp encoding a polypeptide of 373 amino acids, cDNA sequences of both lipA and lipB were cloned and expressed in Escherichia coli BL21 (DE3). The recombinant LipA was mostly expressed as inclusion bodies, and recovered lipase activity at low temperature after in vitro refolded by dilution. Differently, the recombinant LipB was expressed in the soluble form and then purified by Ni-NTA affinity chromatography Column. It showed high lipase activity at low temperature. These results indicated that they were cold-adapted enzymes. This study paves the way for the further research of these cold-adapted lipases for application in the industry.
Base Sequence ; Cloning, Molecular ; Cold Temperature ; Escherichia coli ; metabolism ; Lipase ; genetics ; metabolism ; Open Reading Frames ; Penicillium ; enzymology ; genetics ; Phylogeny ; Polymerase Chain Reaction ; RNA, Ribosomal, 18S ; genetics ; Recombinant Proteins ; genetics ; metabolism