منابع مشابه
Hordeum vulgare Seedlings Amine Oxidase: Purification and Properties.
Although no amine oxidase could be detected in crude extracts, the enzyme has been purified to apparent homogeneity from Hordeum vulgare seedlings using ammonium sulfate precipitation and chromatography on DEAE cellulose, Hydroxylapatite, and Sephadex G200 columns. Gel filtration experiments indicate a molecular weight of about 150,000. The pH optimum of the enzyme was found to be 7.5 in potass...
متن کاملBarley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme.
Oxalate oxidase (EC 1.2.3.4) catalyses the conversion of oxalate and dioxygen into CO(2) and H(2)O(2). The barley (Hordeum vulgare) seedling root enzyme was purified to homogeneity and shown by metal analysis and EPR spectroscopy to contain Mn(II) at up to 0.80 atom per subunit. The involvement of Mn and neither flavin, Cu nor Fe in the direct conversion of dioxygen to H(2)O(2) makes oxalate ox...
متن کاملHaploids in Hordeum Vulgare.
suns. The extension of the Andromeda nebula beyond the photographic limits is presumably typical of what may be found for other such objects. Comparisons with the surface brightness of the galaxy are still hampered by uncertainties in the data for our own system. There may be no part of the galaxy which, seen from outside, would be as bright as the central portion of M 31. In the latter system ...
متن کاملPurification and properties of amine oxidase from pea seedlings
Amine oxidase (EC 1.4.3.6) was purified from pea (Pisum sativum) seedlings with the aim of characterizing its catalytic properties. The specific activity and selectivity of the enzyme were studied with an oxygen sensor by following the kinetics of the amine oxidation reaction, catalysed by the enzyme. The enzyme catalytic constants were calculated from the transient signal of the oxygen sensor ...
متن کاملOxidation of spermine by an amine oxidase from lentil seedlings.
Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in TI-HCI buffer; the K(m) value is 4.4.10(-4) ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 1990
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.93.2.818