Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases (EC 1.2.1.12 and EC 1.2.1.13).
نویسندگان
چکیده
منابع مشابه
D-glyceraldehyde 3-phosphate dehydrogenases of higher plants.
The d-glyceraldehyde 3-P dehydrogenases of spinach leaf, pea seed, and pea shoot were purified. The NADP and NAD-linked enzymes of either spinach leaves and pea shoots could not be separated. Changes in the ratio of NADP- to NAD-linked activity of the spinach leaf and pea shoot enzymes were observed during both purification and storage of crude extracts. The spinach leaf, pea shoot, and pea see...
متن کاملSubunit hybridization of higher plant lactate dehydrogenases
developed a procedure, based on the affinity of all three enzymes for Cibacron Blue 3GA, which allows their simultaneous purification from a cell extract. E. coli K 12, EMG-2 was grown, harvested and disrupted as described by Miller & Stadtman (1972). After treatment with 1% (w/v) streptomycin sulphate, the cell extract was subjected to ammonium sulphate fractionation. The protein fraction prec...
متن کاملec adoption and critical success factors of ec in smes in iran
تجارت الکترونیکی شیوه اجرای مسئولیتها، تقابل با مشتریان و امور معمول عملیاتی در شرکتها را تغییر داده است. تجارت الکترونیکی در عمل تنها خرید و فروش کالاها را از طریق ابزار الکترونیک نمی باشد، بلکه تمام فعالیتهای لازم جهت انجام فرایند فروش را نیز در بر میگیرد. در اواخر دهه 1990 بسیاری از شرکتها فعالیتهای خود را به منظور دستیابی به مشتریان جدید و یا ارائه فرصتهای جدید به مشتریان موجود گسترش دادند...
Nonreversible d-Glyceraldehyde 3-Phosphate Dehydrogenase of Plant Tissues.
Preparations of TPN-linked nonreversible d-glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.9), free of TPN-linked reversible d-glyceraldehyde 3-phosphate dehydrogenase, have been obtained from green shoots, etiolated shoots, and cotyledons of pea (Pisum sativum), cotyledons of peanut (Arachis hypogea), and leaves of maize (Zea mays). The properties of the enzyme were similar from each of the...
متن کاملThe glyceraldehyde 3-phosphate dehydrogenases of liver and muscle. Cooperative interactions and conditions for functional reversibility.
A method is described for the isolation of glyceraldehyde 3.phosphate dehydrogenase from rabbit liver. The enzyme has been crystallized as the NAD complex and its chemical and physical properties have been compared with those of the muscle enzyme. The kinetics of the reversible reaction catalyzed by the dehydrogenases is sensitive to temperature and ionic strength and has been examined at 37, p...
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: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50523-8