نتایج جستجو برای: conformation sensitive gel electrophoresis csge

تعداد نتایج: 431029  

Journal: :jundishapur journal of microbiology 0
mohammad pooideh department of sciences, qom branch, islamic azad university, qom, ir iran ismail jabbarzadeh mycobacteriology department, pasteur institute of iran, tehran, ir iran reza ranjbar molecular biology research center, baqiyatallah university of medical sciences, tehran, ir iran mahnaz saifi mycobacteriology department, pasteur institute of iran, tehran, ir iran; mycobacteriology department, pasteur institute of iran, tehran, ir iran. tel/fax: +98-2166968853

conclusions molecular epidemiology studies of infectious diseases have been useful when bacterial isolates have been clustered in a period of time and in different geographical regions with variable antibiotic resistance patterns. in spite of high geographical differences and different antibiotic resistant patterns, low genetic diversity among the studied tb isolates may refer to the low rate o...

2013
Stefano Perni Matthew Close Clara Franzini-Armstrong

Calsequestrin (CASQ) is the major component of the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscles. This calcium binding protein localizes to the junctional SR (jSR) cisternae where it is responsible for the storage of large amounts of Ca 2+ while it is usually absent, at least in its polymerized form, in the free SR. The retention of CASQ inside the jSR is partly due to its a...

Journal: :Clinical Chemistry and Laboratory Medicine 1972

Journal: :Blood 1996
D Seiffert R R Schleef

The biological functions of vitronectin (Vn) are dependent on its conformation. Whereas plasma Vn is present in a conformation that does not bind to heparin, platelet Vn has been recognized to be in a multimeric, conformationally altered form. To further understand the characteristics of platelet Vn, the molecules present in plasma and total and size-fractionated platelet releasates were compar...

Journal: :The Journal of biological chemistry 1974
U J Hänggi J W Littlefield

Dihydrofolate reductase, isolated from baby hamster kidney cells by affinity chromatography, gave multiple bands on analytical gel electrophoresis and electrofocusing. The number of bands could be reduced to two by forming a complex with the enzyme inhibitor, methotrexate. The two basic enzyme forms, called Form I and Form II, were obtained in large quantities by preparative disc electrophoresi...

2002
JOHN W. LITTLEFIELD

Dihydrofolate reductase, isolated from baby hamster kidney cells by affinity chromatography, gave multiple bands on analytical gel electrophoresis and electrofocusing. The number of bands could be reduced to two by forming a complex with the enzyme inhibitor, methotrexate. The two basic enzyme forms, called Form I and Form II, were obtained in large quantities by preparative disc electrophoresi...

Journal: :Biochimica et biophysica acta 1967
R J McCandliss M D Poling K M Herrmann

The phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate phosphorylating), EC 4.2.1.15) was purified to apparent homogeneity from extracts of Escherichia coli K12. The enzyme has a molecular weight of 140,000 as judged by gel filtration and sedimentation equilibrium analysis. The enzyme...

Journal: :journal of mycology research 2014
sahar javaheri tehrani mansour aliabadian abdolmajid fata mohammad javad najafzadeh

conventional methods for fungal identification in the clinical laboratory rely on morphological andphysiological tests. these tests often need several days or weeks to complete and are frequentlyunspecific. molecular identification mostly implies sequencing, which is relatively expensive andtime-consuming, as well as impractical for large numbers of isolates. the rolling circleamplification app...

2002
Russell J. McCandliss Michael D. Poling Klaus M. Herrmann

The phenylalanine-sensitive 3-deoxy-marabino-heptulosonate ?-phosphate synthase (7-phospho-2-keto-3deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate phosphorylating), EC 4.2.1.15) was purified to apparent homogeneity from extracts of Escherichia coli K12. The enzyme has a molecular weight of 140,000 as judged by gel filtration and sedimentation equilibrium analysis. The enzyme h...

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