Purification of bovine liver S-adenosylhomocysteine hydrolase by affinity chromatography on blue dextran-agarose
β Scribed by Narayanan, Sunanda R.; Borchardt, Ronald T.
- Book ID
- 122522121
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 566 KB
- Volume
- 965
- Category
- Article
- ISSN
- 0304-4165
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UDP-glucose pyrophosphorylase from Golgi apparatus solubilized by detergent has been purified 100-fold from microsomes by affinity chromatography on UTP-agarose. The purified enzyme has apparent Mr 270,000 and isoelectric pH 3.9 against 360,000 and 4.2 for soluble enzyme. According to these characte
## Abstract Recently, several teleost fishes (Perciformes, Cichlidae) have been found that coexpress both a cathodal, liverβspecific and an anodal, eyeβspecific lactate dehydrogenase (LDH), and evidence supporting the hypothesis that these are the products of two distinct genes has been presented (