نتایج جستجو برای: enzymatic lyses

تعداد نتایج: 55202  

Journal: :iranian journal of pharmaceutical sciences 0
mahmood barati department of pharmaceutical biotechnology, school of pharmacy, shahid beheshti university of medical sciences, tehran, iran maryam tabarzad protein technology research center, shahid beheshti university of medical sciences, tehran, iran hossein safarpour pharmaceutical sciences research center, shahid beheshti university of medical sciences, tehran, iran ali ghanbari asad department of medical biotechnology, school of medicine, fasa university of medical sciences, fasa, iran omar ghaderi department of pharmaceutical biotechnology, school of pharmacy, tehran university of medical sciences, tehran, iran

l-asparaginase has remarkable properties which make it useful in dual pharmaceutical and food industries.in this study, simple and advantageous method has been validated for rapid and precise determination of intracellular l-asparaginasein bacterial species. a suspension of bacterial cells was used instead ofcell extract and incubated by substrate (asparagine) after simple wash and centrifugati...

L-Asparaginase has remarkable properties which make it useful in dual pharmaceutical and food industries.In this study, simple and advantageous method has been validated for rapid and precise determination of intracellular L-Asparaginasein bacterial species. A suspension of bacterial cells was used instead ofcell extract and incubated by substrate (asparagine) after simple wash and centrifugati...

2014
Yang Wei Aby A. Thyparambil Yonnie Wu Robert A. Latour

Ribonuclease A (RNase A) is a small globular enzyme that lyses RNA. The remarkable solution stability of its structure and enzymatic activity has led to its investigation to develop a new class of drugs for cancer chemotherapeutics. However, the successful clinical application of RNase A has been reported to be limited by insufficient stability and loss of enzymatic activity when it was coupled...

Journal: :PeerJ 2021

Vibrio parahaemolyticus ( Vp ), a typical microorganism inhabiting marine ecosystems, uses pathogenic virulence molecules such as hemolysins to cause bacterial infections of both human and animals. The thermolabile hemolysin TLH lyses erythrocytes by phospholipase B/A2 enzymatic activity in egg-yolk lecithin. However, few studies have been characterized the biochemical properties use molecular ...

2010
Elena Martínez Giovanna I. Cruz Abenaa M. Brewster Melissa L. Bondy Patricia A. Thompson María Elena Martínez

his commentary, we discuss the challenges and tunities for epidemiologic studies in evaluating cancer as a set of discrete diseases. We show examf the strengths of the case-only design in assessing lative correlation of established risk factors and the ent cancer subtypes. We argue for the use of the nly study design as an important initial step in standing the extent of etiologic heterogeneity...

Journal: :Frontiers in chemistry 2016
E. N. G. Marsh

Journal: :Structure 2000
D Blow

Between 1930 and 1975 biochemical and structural analysis of enzymes led to a clear set of ideas that might form a basis for detailed understanding of enzyme action. Further development required energetic and thermodynamic analysis of enzymes in an aqueous medium, beyond the computational power then available. Structural enzymology advanced in other directions, but the fundamental questions of ...

2017
Eleftherios P. Diamandis Andreas Scorilas A. Scorilas M. Avgeris C. K. Kontos A. Kladi-Skandali G. Papachristopoulou M. Diamantopoulos P. G. Adamopoulos P. Tsiakanikas Bernard Gouget

Journal: :The Biochemical journal 1996
E Asante-Appiah W W Chan

The concurrent effects of two enzyme inhibitors have been analysed previously with the Yonetani-Theorell plot to obtain insight into the interactions between bound inhibitors. This procedure, like many other traditional graphical methods in enzymology, is based on the estimation of intersecting tendencies in a family of lines. In a recent paper from this laboratory [Chan (1995) Biochem. J. 311,...

2014
Hans M. Senn

The halogenases are a group of enzymes that have only come to the fore over the last 10 years thanks to the discovery and characterization of several novel representatives. They have revealed the fascinating variety of distinct chemical mechanisms that nature utilizes to activate halogens and introduce them into organic substrates. Computational studies using a range of approaches have already ...

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