Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotides and aminoacyl-tRNA

1976 ◽  
Vol 172 (1) ◽  
pp. 168-177 ◽  
Author(s):  
Shigekazu Nagata ◽  
Kentaro Iwasaki ◽  
Yoshito Kaziro
Keyword(s):  
Molecular Weight ◽  
Elongation Factor ◽  
Guanine Nucleotides ◽  
Low Molecular Weight ◽  
Elongation Factor 1 ◽  
Molecular Weight Form

scholarly journals The Purification of Low Molecular Weight Form of Polypeptide Elongation Factor 1 from Pig Liver

1974 ◽  
Vol 249 (15) ◽  
pp. 5008-5010
Author(s):  
Kentaro Iwasaki ◽  
Shigekazu Nagata ◽  
Kiyohisa Mizumoto ◽  
Yoshito Kaziro
Keyword(s):  
Molecular Weight ◽  
Elongation Factor ◽  
Low Molecular Weight ◽  
Pig Liver ◽  
Elongation Factor 1 ◽  
Molecular Weight Form

scholarly journals Liver enzyme induction by 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) is accompanied by an increase in the specific activity of elongation factor 1

1978 ◽  
Vol 172 (3) ◽  
pp. 479-486 ◽  
Author(s):  
E T Young ◽  
D M Nicholls
Keyword(s):  
Molecular Weight ◽  
Enzyme Induction ◽  
Sucrose Gradient ◽  
Binding Assay ◽  
Specific Activity ◽  
Elongation Factor ◽  
Low Molecular Weight ◽  
Binding Factor ◽  
The Difference ◽  
Elongation Factor 1

Homogenates of liver were obtained from control rats and from rats that had received DDT [1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane]. The postmicrosomal supernatant fractions were used for the purification of elongation factor 1 by hydroxyapatite chromatography and phosphocellulose chromarography. The amount of binding factor present was essentially the same for both groups of animals, but the specific activity, as measured by the binding assay, was about twice as high in the DDT-treated preparations. After sucrose-gradient sedimentation, the difference in specific activity was found to reside in the low-molecular-weight (50000) form of elongation factor 1. The implications of an increased reactivity of elongation factor 1 during the induction of membrane enzymes are discussed.

scholarly journals The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

1980 ◽  
Vol 189 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Yoav Ben-Yoseph ◽  
Melinda Hungerford ◽  
Henry L. Nadler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Krabbe Disease ◽  
Low Molecular Weight ◽  
Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

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