Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
نویسندگان
چکیده
منابع مشابه
Purification of Bacteriophage T4 Lysozyme*
The lysozyme of bacteriophage T4 was purified to apparent homogeneity from lysates of the phage grown on Escherichia coli. The enzyme is a single polypeptide chain of molecular weight 19,000, with a single NH&erminal methionine residue and a single COOH-terminal leuciue residue. The amino acid composition of the protein was determined. The phage lysozyme exhibits a much greater specific activit...
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Protein aggregation is a problem in biotechnology. High temperature is one of the most important reasons to enhance enzyme inactivation and aggregation in industrial systems. This work focuses on the effect of TiO2 and SiO2 nanoparticles on refolding and reactivation of lysozyme. In the presence of TiO2 and SiO2 nanoparticles, after enzyme heat treatm...
متن کاملProcessing of the tail lysozyme (gp5) of bacteriophage T4.
The processing site of gp5 has been determined to be between residues Val-390 and His-391, instead of Ser-351 and Ala-352 as previously reported (H. Kanamaru, N. C. Gassner, N. Ye, S. Takeda, and F. Arisaka, J. Bacteriol. 181:2739-2744). Moreover, the maturation of gp5 is abolished by null mutations in other hub genes, indicating that cleavage requires the interactions of several baseplate prot...
متن کاملBacteriophage T4 DNA-dependent in vitro synthesis of lysozyme.
A cell-free system derived from uninfected Escherichia coli previously was shown to synthesize beta-glucosyl transferase in response to T4 DNA. This same in vitro system, when incubated at slightly higher magnesium concentrations, also synthesized enzymatically active lysozyme. The lysozyme activity that appeared was judged to be T4-specific since antibodies prepared against authentic T4-lysozy...
متن کاملThe three dimensional structure of the lysozyme from bacteriophage T4.
The three dimensional structure of the lysozyme from bacteriophage T4 has been determined from a 2.5 A resolution electron density map. About 60% of the molecule is in a helical conformation and there is one region consisting of antiparallel beta-structure. The polypeptide backbone folds into two distinct lobes linked in part by a long helix. In the region between the two lobes, there is a clef...
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ژورنال
عنوان ژورنال: Biopolymers
سال: 1987
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.360260505