A proposed nucleotide sequence for the 5S ribosomal ribonucleic acid of rainbow trout (Salmo gairdneri)

1978 ◽  
Vol 56 (1) ◽  
pp. 60-65 ◽  
Author(s):  
Kenneth L. Roy

Rainbow trout cell cultures have been exposed to 32P-labelled inorganic phosphate and the labelled RNA has been isolated. The 5S ribosomal ribonucleic acid (5S rRNA) was purified by polyacrylamide gel electrophoresis, then digested with RNase T1 or pancreatic RNase. The products of complete digestion were separated and their sequences determined. These analyses have allowed a sequence to be proposed which differs in eight positions from that of mammalian 5S rRNAs.

1976 ◽  
Vol 153 (2) ◽  
pp. 437-446 ◽  
Author(s):  
N J Holness ◽  
G Atfield

1. The nucleotide chain of tRNA Cys from baker's yeast was readily split at the anticolon into two large fragments by brief treatment with ribonuclease T1.2. The whole molecule and the two derived large fragments were completely digested with (a) pancreatic ribonuclease and (b) ribonuclease T1. The fragments present in each of the digests were separated and sequenced by conventional methods. 3. The groups of fragments derived from the two methods of digestion were entirely compatible with each other. 4. The molecule is 75 nucleotides long, but, as isolated, lacks the terminal adenosine and the neighboring cytidylic acid residue. The minor nucleotides 1-methyladenylic acid, 7-methylguanylic acid, 5-methylcytidylic acid and N6 (γγ-dimethylallyl)adenylic acid (isopentenyladenylic acid) were identified.


1975 ◽  
Vol 21 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Catherine Adapoe ◽  
Marvin Silver

Adenosine triphosphatase (ATPase) from Thiobacilhis ferrooxidans was purified 55-fold. Polyacrylamide gel electrophoresis of the most purified fraction showed only one major band; histochemical analysis showed that the ATPase activity was associated with this band. The pH optimum is 9–10. The enzyme hydrolyzed ATP stoichiometrically to ADP and inorganic phosphate, the Km for this substrate being 7.75 × 10−3 M. GTP and ITP are alternate substrates, the Km values for these being 6.71 × 10−3 M and 3.12 × 10−3 M, respectively. ADP is slightly hydrolyzed. Magnesium, manganese, and calcium can serve as cofactors; Km values for these are 2.0 × 10−3 M, 9.4 × 10−4 M, and 8.0 × 10−4 M, respectively. The enzyme activity was not activated by either sodium or potassium, but a combination of the two ions were inhibitory. Azide and p-hydroxymercuribenzoate strongly inhibited the enzyme activity, whereas cyanide, dinitrophenol, and N, N′-dicyclohexylcarbodiimide (DCCD) were without effect. The enzyme was cold labile at 0 °C, but was more stable at 18–24 °C.


FEBS Letters ◽  
1975 ◽  
Vol 54 (2) ◽  
pp. 241-244 ◽  
Author(s):  
T.A. Walker ◽  
J.L. Betz ◽  
J. Olah ◽  
N.R. Pace

1986 ◽  
Vol 34 (10) ◽  
pp. 4190-4194 ◽  
Author(s):  
KAZUNOBU MIURA ◽  
JUNJI KAKUCHI ◽  
ERIKO ENDO ◽  
TOHRU UEDA ◽  
KUNIHIKO KOBAYASHI ◽  
...  

Biochemistry ◽  
1983 ◽  
Vol 22 (25) ◽  
pp. 5858-5868 ◽  
Author(s):  
Robert McCarroll ◽  
Gary J. Olsen ◽  
Yvonne D. Stahl ◽  
Carl R. Woese ◽  
Mitchell L. Sogin

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