نتایج جستجو برای: excremental coli form
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Title of Document: BIOFILM FORMATION BY ESCHERICHIA COLI O157:H7 Karen Suzanne Silagyi, M.S., 2007 Directed By: Associate Professor, Dr. Y. Martin Lo, Nutrition and Food Science Escherichia coli O157:H7 from cattle was evaluated for its ability to produce biofilm on food contact surfaces and quorum sensing signals in various raw meat, raw poultry, and produce broths. Generally, the strain was a...
the human papillomavirus l1 major capsid protein (hpv l1), the basis of the current vaccines, self-assembles into virus-like particles (vlps). herein, we describe the expression and purification of recombinant hpv16 l1 in e. coli system. the l1 protein was generated in a fused form using an inducible expression system. the recombinant gst-l1 fusion protein migrated as a 82 kda protein in sds-pa...
BACKGROUND The tdk gene (encoding deoxythymidine kinase) of the gamma-proteobacterium Xenorhabdus nematophila has two potential translation start sites. The promoter-distal start site was predicted to be functional based on amino acid sequence alignment with closely related Tdk proteins. However, to experimentally determine if either of the two possible start codons allows production of a funct...
Background and Aims: Enzybiotics are probably the future line of weapons against drug resistant bacteria. They lyse bacteria with the new mechanisms with few likelihood of generating resistance. LasA, which is secreted from Pseudomonas strains degrades Staphylococcus aureus (S. aureus) cell wall and has the potential to use against drug resistant S. aureus infections. Materials and Metho...
The existence of a free form of a specific lipoprotein of molecular weight 7,200 was examined in the envelopes of several gram-negative bacteria. When the envelope proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis, distinct peaks were observed in Salmonella typhimurium, Serratia marcescens, and Pseudomonas aeruginosa at the same position as the free form of the...
Selection of a system for successful recombinant protein production is important. The aim of this study wasto produce high levels of human interleukin-2 (hIL-2) in soluble form. To this end, the pET32a vector inEscherichia coli BL21 (DE3) was used as an expression system, since it was previously used for the productionof mouse IL-2 in soluble form. The results indicated that c...
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