Production and Heat Stability of Staphylococcal Nuclease
نویسندگان
چکیده
منابع مشابه
Effect of anaerobiosis on staphylococcal nuclease production.
Five strains of Staphylococcus aureus were examined quantitatively for the production of nuclease under aerobic and anaerobic conditions. Hydrolysis of deoxyribonucleic acid and ribonucleic acid was detected by measuring the release of acidsoluble nucleotides spectrophotometrically. We found that the enzyme was produced anaerobically, as well as aerobically, and that anaerobiosis had no effect ...
متن کاملThe role of tryptophan in staphylococcal nuclease stability.
Staphylococcal nuclease (SNase) has a single Trp residue at position 140. Circular dichroism, intrinsic and ANS-binding fluorescence, chemical titrations and enzymatic assays were used to measure the changes of its structure, stability and activities as the Trp was mutated or replaced to other positions. The results show that W140 is critical to SNase structure, stability, and function. Mutants...
متن کامل[Cold denaturation of staphylococcal nuclease].
It has been shown that the structure of staphylococcal nuclease breaks down reversibly both at a temperature increase above 20 degrees C and at its decrease. Both the heat and cold denaturations of protein are well approximated by a transition between two states differing in heat capacity, which means that the whole protein molecule represents a unique cooperative system with a well developed h...
متن کاملStaphylococcal nuclease: sequential assignments and solution structure.
Sequential assignments are reported for backbone 15N and 1H of nearly all residues of staphylococcal nuclease (Nase) complexed with thymidine 3',5'-diphosphate and Ca2+. Because of the relatively large size of the Nase ternary complex, Mr 18K, the crucial element of our assignment strategy was the use of isotope-edited two-dimensional NMR spectra, particularly 15N-edited nuclear Overhauser enha...
متن کاملCrowding effects on the temperature and pressure dependent structure, stability and folding kinetics of Staphylococcal Nuclease.
FT-IR spectroscopic, small-angle X-ray scattering and calorimetric measurements have been applied to explore the effect of the macromolecular crowder agent Ficoll on the temperature- and pressure-dependent stability diagram and folding reaction of the protein Staphylococcal Nuclease (SNase). Additionally, we compare the experimental data with approximate theoretical predictions. We found that t...
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ژورنال
عنوان ژورنال: Applied Microbiology
سال: 1973
ISSN: 0003-6919
DOI: 10.1128/am.25.3.332-336.1973