Extracts prepared from a variety of higher plant tissues have been examined for L-aminoacid:2-glyoxylate aminotransferase (glyoxylate transaminase) activity. This enzyme has been detected in extracts prepared from sunflower cotyledons, corn coleoptiles, mature pea leaves, and carrot storage tissues. Measurement of glyoxylate transaminase activity was based on ability of the extracts to convert glyoxylate- 1,2-C14 to glycine-1,2-C14 in the presence of a suitable amino group donor. Properties of this enzyme system, including amino donor requirements, inhibition, pH optima, and reversibility, have been studied using extracts prepared from mature pea leaves. In sunflower cotyledons, glyoxylate transaminase activity decreased during germination....
A transamidinase was purified 463-fold from Lathyrus sativus seedlings by affinity chromatography on...
Information about amino acids synthesized by plants, their functions in amino acid metabolism, the p...
Two isoenzymes of leucine aminotransferase (LAT I and LAT II) were extracted and partially purified ...
Extracts prepared from a variety of higher plant tissues have been examined for L-aminoacid:2-glyoxy...
The activity of glutamic acid aminotransferase with respect to six keto acids was studied in dialyse...
1. [14C2] glyoxylate was rapidly metabolized by carrot storage tissues, pea leaves, pea cotyledons, ...
Alanine aminotransferase from germinating castor bean endosperms was purified about 1,500-fold by am...
AbstractGlutamate asmialdehyde aminotransferase, a key enzyme in the synthetic pathway leading to ch...
Extract from ungerminated bean seeds (Phaseolus vulgaris L. cv. Saxa) was fractionated by gel chroma...
The NADPH-dependent conversion of amino acids to their aldoximes is an initial step in glucosinolate...
Aminotransferases are pyridoxal-5'-phosphate dependent enzymes that transfer amino groups from amino...
In 1927 Dorothy Needham (l), observed that when glutamic acid was added to minced pigeon breast musc...
Cotyledons of germinating sunflower, pumpkin, linseed, and watermelon seeds and the endosperm of ger...
One of the less well-known aspects of glutathione (GSH) metabolism is its degradation. Two pathways ...
The cormatographic study of the free amino acids existing in Opuntia vulgaris (stem and fruit), Cere...
A transamidinase was purified 463-fold from Lathyrus sativus seedlings by affinity chromatography on...
Information about amino acids synthesized by plants, their functions in amino acid metabolism, the p...
Two isoenzymes of leucine aminotransferase (LAT I and LAT II) were extracted and partially purified ...
Extracts prepared from a variety of higher plant tissues have been examined for L-aminoacid:2-glyoxy...
The activity of glutamic acid aminotransferase with respect to six keto acids was studied in dialyse...
1. [14C2] glyoxylate was rapidly metabolized by carrot storage tissues, pea leaves, pea cotyledons, ...
Alanine aminotransferase from germinating castor bean endosperms was purified about 1,500-fold by am...
AbstractGlutamate asmialdehyde aminotransferase, a key enzyme in the synthetic pathway leading to ch...
Extract from ungerminated bean seeds (Phaseolus vulgaris L. cv. Saxa) was fractionated by gel chroma...
The NADPH-dependent conversion of amino acids to their aldoximes is an initial step in glucosinolate...
Aminotransferases are pyridoxal-5'-phosphate dependent enzymes that transfer amino groups from amino...
In 1927 Dorothy Needham (l), observed that when glutamic acid was added to minced pigeon breast musc...
Cotyledons of germinating sunflower, pumpkin, linseed, and watermelon seeds and the endosperm of ger...
One of the less well-known aspects of glutathione (GSH) metabolism is its degradation. Two pathways ...
The cormatographic study of the free amino acids existing in Opuntia vulgaris (stem and fruit), Cere...
A transamidinase was purified 463-fold from Lathyrus sativus seedlings by affinity chromatography on...
Information about amino acids synthesized by plants, their functions in amino acid metabolism, the p...
Two isoenzymes of leucine aminotransferase (LAT I and LAT II) were extracted and partially purified ...