scholarly journals Respon Pertumbuhan Dan Produksi Beberapa Varietas Kacang Hijau (Phaseolus aureus) Akibat Perlakuan Pemupukan

2017 ◽  
Vol 21 (1) ◽  
pp. 68-77
Author(s):  
Mukhtar Yusuf ◽  
Keyword(s):  
Phaseolus Aureus

scholarly journals Phosphorylation of d-Galactose and l-Arabinose by Extracts from Phaseolus aureus Seedlings

1960 ◽  
Vol 235 (4) ◽  
pp. 906-909 ◽  
Author(s):  
Elizabeth F. Neufeld ◽  
David S. Feingold ◽  
W.Z. Hassid
Keyword(s):  
Phaseolus Aureus

scholarly journals The Biosynthesis of Sucrose and Nucleoside Diphosphate Glucoses in Phaseolus aureus

1970 ◽  
Vol 45 (6) ◽  
pp. 782-786 ◽  
Author(s):  
Deborah P. Delmer ◽  
Peter Albersheim
Keyword(s):  
Phaseolus Aureus

Influence of IBA and Cordycepin on Rooting and RNA Synthesis in Stem Cuttings of Phaseolus aureus Roxb

1983 ◽  
Vol 24 (2) ◽  
pp. 139-146 ◽  
Author(s):  
B. C. Jarvis ◽  
P. R. M. Shannon ◽  
S. Yasmin
Keyword(s):  
Rna Synthesis ◽  
Stem Cuttings ◽  
Phaseolus Aureus

scholarly journals SOME PROTEINS FROM THE MUNG BEAN, PHASEOLUS AUREUS ROXBURGH

1920 ◽  
Vol 44 (2) ◽  
pp. 303-317
Author(s):  
Carl O. Johns ◽  
Henry C. Waterman
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus

scholarly journals INVESTIGATIONS ON THE MUNG BEAN (PHASEOLUS AUREUS ROXBURGH)

1948 ◽  
Vol 175 (1) ◽  
pp. 377-383
Author(s):  
W. Edward Belton ◽  
Cecile A. Hoover
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus

scholarly journals Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum

1965 ◽  
Vol 97 (1) ◽  
pp. 112-124 ◽  
Author(s):  
PJ Peterson ◽  
L Fowden
Keyword(s):  
Carboxylic Acid ◽  
Enzyme Preparation ◽  
Enzymic Activity ◽  
The Other ◽  
Asparagus Officinalis ◽  
Acid Activation ◽  
Phaseolus Aureus ◽  
Substrate Specificities ◽  
Imino Acids ◽  
Ammonium Sulphate Fractionation

1. A prolyl-s-RNA synthetase (prolyl-transfer RNA synthetase) has been purified about 250-fold from seed of Phaseolus aureus (mung bean), a species not producing azetidine-2-carboxylic acid, and more than 10-fold from rhizome apices of Polygonatum multiflorum, a liliaceous species containing azetidine-2-carboxylic acid. The latter enzyme was unstable during ammonium sulphate fractionation. 2. The enzymes exhibited different substrate specificities towards the analogue. That from Phaseolus, when assayed by the ATP-PP(i) exchange, showed azetidine-2-carboxylic acid activation at about one-third the rate with proline. Both labelled imino acids gave rise to a labelled aminoacyl-s-RNA. The enzyme from Polygonatum, however, activated only proline. 3. The enzyme from Polygonatum also formed a labelled prolyl-s-RNA with Phaseolus s-RNA but at a lower rate than when the Phaseolus enzyme was used. No reaction occurred when the Phaseolus enzyme was coupled with Polygonatum s-RNA, and only a very slight one was observed when both enzyme and s-RNA came from Polygonatum. 4. Protein preparations from seeds of Pisum sativum, another species not producing azetidine-2-carboxylic acid, also activated the analogue in addition to proline, whereas those from rhizome and seeds of Convallaria, the species from which the analogue was originally isolated, failed to activate it. However, a liliaceous species not producing the analogue, Asparagus officinalis, activated it. 5. Of the other proline analogues investigated, only 3,4-dehydro-dl-proline and l-thiazolidine-4-carboxylic acid were active with the enzyme preparation from Phaseolus. 6. pH optima of 7.9 and 8.4 were established for the enzymes from Phaseolus and Polygonatum respectively. 7. The Phaseolus enzyme was specific for ATP and PP(i). Mn(2+) partially replaced the requirement for Mg(2+) as cofactor. Preincubation with p-chloromercuribenzoate at a concentration of 0.5mm or higher produced over 99% inhibition of the Phaseolus enzyme. One-half the enzymic activity was destroyed by preheating for 5min. at 62 degrees in tris-hydrochloric acid buffer, pH7.9. 8. All experimental evidence supports the hypothesis that azetidine-2-carboxylic acid and proline are activated by the same enzyme in Phaseolus preparations, whereas the analogue was inactive in all Polygonatum preparations. The possible nature of this different substrate behaviour is discussed.

Comparison of the conformation and stability of the native dimeric, monomelic, tetrameric and the desensitized forms of the nucleotide pyrophosphatase from mung bean (Phaseolus aureus) seedlings

1980 ◽  
Vol 2 (3) ◽  
pp. 211-225 ◽  
Author(s):  
A. R. Venugopala Reddy ◽  
C. V. Balakrishnan ◽  
J. Sobhanaditya ◽  
S. D. Ravindranath ◽  
V. S. Ananthanarayanan ◽  
...  
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus ◽  
Nucleotide Pyrophosphatase

scholarly journals The Formation of β, 1 → 4 Glucan from UDP-α-d-Glucose Catalyzed by a Phaseolus aureus Enzyme

1972 ◽  
Vol 50 (3) ◽  
pp. 371-374 ◽  
Author(s):  
A. F. Clark ◽  
C. L. Villemez
Keyword(s):  
Phaseolus Aureus

scholarly journals Interaction of soluble glucosyl- and mannosyl-transferase enzyme activities in the synthesis of a glucomannan

1972 ◽  
Vol 129 (3) ◽  
pp. 645-655 ◽  
Author(s):  
J. S. Heller ◽  
C. L. Villemez
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Enzyme Preparation ◽  
The Other ◽  
Acceptor Molecule ◽  
Soluble Enzyme ◽  
Phaseolus Aureus ◽  
Polymeric Product ◽  
Sugar Nucleotide ◽  
Solubilized Enzyme

A neutral-detergent-solubilized-enzyme preparation derived from Phaseolus aureus hypocotyls contains two types of glycosyltransferase activity. One, mannosyltransferase enzyme activity, utilizes GDP-α-d-mannose as the sugar nucleotide substrate. The other, glucosyltransferase enzyme activity, utilizes GDP-α-d-glucose as the sugar nucleotide substrate. The soluble enzyme preparation catalyses the formation of what appears to be a homopolysaccharide when either sugar nucleotide is the only substrate present. A β-(1→4)-linked mannan is the only polymeric product when only GDP-α-d-mannose is added. A β-(1→4)-linked glucan is the only polymeric product when only GDP-α-d-glucose is added. In the presence of both sugar nucleotides, however, a β-(1→4)-linked glucomannan is formed. There are indications that endogenous sugar donors may be present in the enzyme preparation. There appear to be only two glycosyltransferases in the enzyme preparation, each catalysing the transfer of a different sugar to the same type of acceptor molecule. The glucosyltransferase requires the continual production of mannose-containing acceptor molecules for maintenance of enzyme activity, and is thereby dependent upon the activity of the mannosyltransferase. The mannosyltransferase, on the other hand, does not require the continual production of glucose-containing acceptors for maintenance of enzyme activity, but is severely inhibited by GDP-α-P-glucose. These properties promote the synthesis of β-(1→4)-linked glucomannan rather than β-(1→4)-linked glucan plus β-(1→4)-linked mannan when both sugar nucleotide substrates are present.

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