METABOLISM OF C14-LABELED GLYCINE, l-HISTIDINE, l-LEUCINE, AND l-LYSINE
نویسندگان
چکیده
منابع مشابه
The uptake in vitro of C14-labeled glycine, l-leucine, and l-lysine by different components of guinea pig liver homogenate.
We have reported (1) that n-lysine labeled with Cl4 can be incorporated into the proteins of guinea pig liver homogenate under two different conditions. In the one case the enzyme used was the whole homogenate, the optimum pH was near 6.2, there was an obligatory requirement of calcium, and the incorporation was independent of oxygen. This set of conditions is designated below as the “acid calc...
متن کاملSynthesis of C14-Labeled L-Sorbose and L-Ascorbic Acid
A m ethod is prese nted for preparing C'4-l abeled L-ascorbi c acid (vi tamin C) from labeled banum D-gluconate or D-glucose. The process is adapted from t he commercial synthesis of vi tamin C t hrough sorbitol, L-sorbose and potassium di-O-isopropylidene-2kelo-L-guloll.ate. In .th e cyanohydrin . synt hesis of labeled D-glucose, barium D-gluconate is used as an lI1term ed~at~ . Fo: prepanng l...
متن کاملThe metabolism of ring-labeled L-thyroxine-C14 in vivo.
In the past, investigators have used thyroxine labeled either with JIP" in the 3',5'-position or with C14 in the carboxyl position to study the metabolism of thyroxine in vivo. Although these studies have yielded much valuable information, our knowledge about the metabolic fate of the ring structure in thyroxine is incomplete because both the 3'5'-IJ13 and the carboxyl-C14 are rapidly removed f...
متن کاملThe Mammalian Metabolism of L-Histidine
The major pathway of histidine metabolism in animals and bacteria other than incorporation into protein involves first deamination to urocanic acid, then the anaerobic addition of water to form an intermediate generally considered to be 4(5)imidazolone-5(4)-propionic acid (1, 2). Finally, the ring is split enzymatically to ~formiminoglutamic acid (3) which is converted to free cglutamic acid by...
متن کاملl-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr.
Studies have been conducted with the arginase (l-arginine amidinohydrolase, EC 3.5.3.1) of two legumes: jack bean, Canavalia ensiformis (L.) DC., a l-canavanine-containing plant and soybean, Glycine max, a canavanine-free species. Analyses of the arginase obtained from gradient-purified mitochondria of these legumes revealed that the arginine-dependent (ADA) and canavanine-dependent activities ...
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: 1950
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)56230-x