Crystallization of Pyridoxamine-5'-phosphate at Isoelectric Point
نویسندگان
چکیده
منابع مشابه
The interaction of pyridoxamine 5-phosphate with aspartate aminotransferase.
The binding of pyridoxamine 5-phosphate to the enzyme aspartate aminotransferase from pig heart was investigated by fluorescence spectroscopy. The substantial decrease in fluorescence intensity at 390 rnp that follows the interaction of pyridoxamine 5-phosphate with the apoenzyme was used to determine the alhnity constant. The effect of pH on the stability of the apoenzyme-pyridoxamine 5-phosph...
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We report the purification and enzymological characterization of Escherichia coli K-12 pyridoxine (pyridoxamine) 5'-phosphate (PNP/PMP) oxidase, which is a key committed enzyme in the biosynthesis of the essential coenzyme pyridoxal 5'-phosphate (PLP). The enzyme encoded by pdxH was overexpressed and purified to electrophoretic homogeneity by four steps of column chromatography. The purified Pd...
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Measurements have been made at 40 degrees C. of the osmotic pressure and viscosity of 1 per cent gelatin solutions containing varying amounts of hydrochloric acid or sodium hydroxide. Each property was found to exhibit a decided minimum near pH 4.7. In the osmotic pressure experiments the pH of the inside solutions was greater than that of the outside solutions at pH values below 4.7, while it ...
متن کاملMechanism of binding of pyridoxamine 5-phosphate to the apoenzyme aspartate aminotransferase. Fluorescence studies.
The combination of pyridoxamine 5-phosphate with the apoprotein of the enzyme aspartate aminotransferase has been followed by measuring the quenching of protein fluorescence associated with complex formation. The reaction takes place in two steps; an initial rapid decrease in protein fluorescence is followed by a slow quenching process which parallels the recovery of catalytic activity. Similar...
متن کاملPyridoxamine-5'-phosphate oxidase exhibits no specificity in prochiral hydrogen abstraction from substrate.
The stereochemistry for hydrogen removal from pyridoxamine 5'-phosphate with liver pyridoxine (pyridoxamine)-5'-phosphate oxidase was examined to determine whether or not there are significant steric constraints at the substrate region of the active site of the oxidase. For this, pyridoxal 5'-phosphate was reduced with tritium-labeled sodium borohydride in ammoniacal solution to yield racemical...
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ژورنال
عنوان ژورنال: The Journal of the Society of Chemical Industry, Japan
سال: 1966
ISSN: 0023-2734,2185-0860
DOI: 10.1246/nikkashi1898.69.6_1259