Calmodulin-like proteins from Escherichia coli
نویسندگان
چکیده
منابع مشابه
In silico Study of Toll-Like Receptor 4 Binding Site of FimH from Uropathogenic Escherichia coli
Introduction : The innate immune system as the first line of defense against the pathogens recognizes pathogen-associated molecular patterns (PAMPs) by Toll-Like Receptors (TLRs). Interaction of bacterial PAMPs by TLRs results in activation of innate and acquired immunity. FimH adhesin, a minor component of type 1 fimbriae encoded by Uropathogenic Escherichia coli (UPEC) is a PAMP of TLR4 tha...
متن کاملHistone-like proteins in the purified Escherichia coli deoxyribonucleoprotein.
Analysis of E.coli chromosomes isolated under conditions similar to those used for isolation of eukaryotic chromatin has shown that: 1) The proteins of highly purified E.coli deoxyribonucleoprotein are mainly in addition to RNA polymerase two specific histone-like proteins of apparent molecular weight of 17,000 and 9,000 (proteins 1 and 2, respectively). 2) Proteins 1 and 2 occur in approximate...
متن کاملEscherichia coli heat-shock proteins
lstituto di Microbiologia’ and lstituto di Clinica Dermosif ilopaticaz, Seconda Universita degli Studi di Napoli, Facolta di Medicina e Chirurgia, Larghetto S.Aniello a Caponapoli, 2,801 38 Napoli, Italy Bacterial heat-shock proteins (HSPs) from Escherichia co/i (GroES, GroEL and DnaK) were studied for their ability to induce by themselves the expression and release of tumour necrosis factor-a ...
متن کاملProducing GST-Cbx7 Fusion Proteins from Escherichia coli
This protocol describes the production of GST-Cbx7 fusion proteins from E. coli, originally developed in the recent publication (Zhen et al., 2016). The pGEX-6P-1-GST plasmids encoding the Cbx7 variants were transformed into BL21 competent cells. The fusion protein production was induced by isopropyl-beta-D-thiogalactopyranoside and they were purified by Glutathione Sepharose 4B. This protocol ...
متن کاملExtraction and isolation of individual ribosomal proteins from Escherichia coli.
We have described a new method for the quantitative separation of ribosomal proteins and ribosomal ribonucleic acid. A procedure for the preparation of individual ribosomal proteins by polyacrylamide gel electrophoresis is also described. By the use of gels with smaller pores, at least four of the electrophoretic components from the 30S ribosome can be split into additional protein fractions. B...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1981
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)54526-7