نتایج جستجو برای: aspartat amino transferase

تعداد نتایج: 233784  

Journal: :The Biochemical journal 1997
P Sacchetta R Petruzzelli S Melino T Bucciarelli A Pennelli F Amicarelli M Miranda C Di Ilio

پایان نامه :دانشگاه آزاد اسلامی - دانشگاه آزاد اسلامی واحد مرودشت - دانشکده علوم پایه 1392

چکیده: خواص مولکولی 5کمپلکسni(ii) شیف باز که شامل کره کئوردیناسیون nnos: methyl-2-{n-[2-(acetone)triflourolidynenitrilo]ethyl}amino-1-yclopentenedithi-ocarboxylate l1= methyl-2-{n-[2-(acetone)ethylidyneni-trilo]ethyl}amino-1-lopentenedithi-ocarboxylate l2= methyl-2-{n-[2-(acetone)phenylidy-nenitrilo]ethyl}amino-1-cyclopentenedithi-ocarboxylate l3= methyl-2-{[1-methyl-2-(ace-tone)ethylid...

Journal: :Cancer research 1987
T Kano M Sakai M Muramatsu

We have used a rat glutathione S-transferase P (GST-P) complementary DNA as a probe to screen a human placenta complementary DNA library constructed in the lambda gt11 vector. One of the positive clones contained the complete coding region (630 base pair) and the entire 3'-noncoding region (78 base pair) of the putative human glutathione S-transferase pi (GST-pi) subunit mRNA. From the nucleoti...

2001
Chi-Yu Lee Lynt Johnson

Three major forms of cytosolic glutathione S-transferase (designated F1, F2, and F3 transferases according to increasing isoelectric points) were purified to homogeneity from liver of DBA/2J mice, primarily by CM-cellulose and hydroxylapatite chromatography. The purified enzymes were shown to have specific activities of 104, 281, and 143 units/mg, respectively, when assayed with 1 m~ each of l-...

2003
ROBIN BROWN

I t has been shown in previous communications that, in the presence of the specific cofactor nicotinamide adenine dinucleotide (NAD), diphtheria toxin inhibits the transfer of amino acids from aminoacyl-tRNA to the growing polypeptide chains on the ribosomes in cell-free extracts from mammalian cells (1). Although bacterial cell extracts axe completely insensitive to inhibition (1), toxin and N...

Journal: :The Biochemical journal 1980
Y C Awasthi D D Dao R P Saneto

Human liver glutathione S-transferases (GSH S-transferases) were fractionated into cationic and anionic proteins. During fractionation with (NH4)2SO4 the anionic GSH S-transferases are concentrated in the 65%-saturated-(NH4)2SO4 fraction, whereas the cationic GSH S-transferases separate in the 80%-saturated-(NH4)2SO4 fraction. From the 65%-saturated-(NH4)2SO4 fraction two new anionic GSH S-tran...

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