RIBONUCLEASE ACTIVITY OF FISH MUSCLE EXTRACTS

1958 ◽  
Vol 36 (6) ◽  
pp. 633-643 ◽  
Author(s):  
Neil Tomlinson
Keyword(s):  
Ribonucleic Acid ◽  
Fish Muscle ◽  
Ribonuclease Activity ◽  
Phosphodiesterase Activity ◽  
Ph Optimum ◽  
Ophiodon Elongatus ◽  
Zone Electrophoresis

A ribonuclease was partially purified from muscle of lingcod (Ophiodon elongatus). The preparation degraded yeast and lingcod ribonucleic acid. Four 3′-mononucleotides were identified as digestion products. The enzyme was readily destroyed by heat and acid (10 minutes at 58 °C, pH 2.5), and was inhibited strongly by Zn++, Cu++, monoiodoacetate, formaldehyde, and NaF. Its pH optimum was 6.5. Ribonuclease activity was also demonstrated in muscle extracts from spring salmon, lemon sole, dogfish, sculpin, herring, and swordfish. The muscle extracts of all fish examined possessed phosphodiesterase activity. The ribonuclease in lingcod extract could be separated from two phosphodiesterases also present by zone electrophoresis.

RIBONUCLEASE ACTIVITY OF FISH MUSCLE EXTRACTS

1958 ◽  
Vol 36 (1) ◽  
pp. 633-643 ◽  
Author(s):  
Neil Tomlinson
Keyword(s):  
Ribonucleic Acid ◽  
Fish Muscle ◽  
Ribonuclease Activity ◽  
Phosphodiesterase Activity ◽  
Ph Optimum ◽  
Ophiodon Elongatus ◽  
Zone Electrophoresis

A ribonuclease was partially purified from muscle of lingcod (Ophiodon elongatus). The preparation degraded yeast and lingcod ribonucleic acid. Four 3′-mononucleotides were identified as digestion products. The enzyme was readily destroyed by heat and acid (10 minutes at 58 °C, pH 2.5), and was inhibited strongly by Zn++, Cu++, monoiodoacetate, formaldehyde, and NaF. Its pH optimum was 6.5. Ribonuclease activity was also demonstrated in muscle extracts from spring salmon, lemon sole, dogfish, sculpin, herring, and swordfish. The muscle extracts of all fish examined possessed phosphodiesterase activity. The ribonuclease in lingcod extract could be separated from two phosphodiesterases also present by zone electrophoresis.

scholarly journals Alkaline ribonuclease and phosphodiesterase activity in rat liver plasma membranes

1973 ◽  
Vol 132 (3) ◽  
pp. 449-458 ◽  
Author(s):  
Terence D. Prospero ◽  
Malcolm L. E. Burge ◽  
Kenneth A. Norris ◽  
Richard H. Hinton ◽  
Eric Reid
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Gradient Centrifugation ◽  
Ribonuclease Activity ◽  
Nuclear Fraction ◽  
Phosphodiesterase Activity ◽  
Ph Optimum ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

The ribonuclease and phosphodiesterase activities of rat liver plasma membranes, purified from the crude nuclear fraction by centrifugation in an A-XII zonal rotor and flotation, were examined and compared. The plasma membrane is responsible for between 65 and 90% of the phosphodiesterase activity of the cell and between 25 and 30% of the particulate ribonuclease activity measured at pH8.7 in the presence of 7.5mm-MgCl2. Both enzymes were most active between pH8.5 and 8.9. Close to the pH optimum, both enzymes were more active in Tris buffer than in Bicine or glycine buffer. Both plasma-membrane phosphodiesterase and ribonuclease were strongly activated by Mg2+, there being at least a 12-fold difference between the activity in the presence of Mg2+ and of EDTA. There is, however, a difference in the response of the enzymes to Mg2+ and EDTA in that the phosphodiesterase is fully activated by 1.0mm-MgCl2 and fully inhibited by 1.0mm-EDTA, whereas the ribonuclease requires 7.5mm-MgCl2 for full activation and 5mm-EDTA for full inhibition. Density-gradient centrifugation has indicated that on solubilization in Triton X-100 most of the ribonuclease activity is released into a small fragment of the same size as that containing the phosphodiesterase activity. The relationship between the two activities is discussed in view of these results.

LINGCOD MUSCLE NUCLEASE

1959 ◽  
Vol 37 (8) ◽  
pp. 945-952 ◽  
Author(s):  
Neil Tomlinson
Keyword(s):  
Ribonucleic Acid ◽  
Free Base ◽  
Ophiodon Elongatus ◽  
Base Form ◽  
Nitrophenyl Phosphate ◽  
Diethylaminoethyl Cellulose ◽  
Cyclic Phosphates ◽  
Low Rate

A nuclease from muscle of lingcod (Ophiodon elongatus) has been purified by chromatography on diethylaminoethyl cellulose in the free-base form by stepwise elution with increasing concentrations of tris(hydroxymethyl)aminomethane. HCl, pH 7.0. The nuclease has been shown to hydrolyze ribonucleic acid, adenosine 3′-benzyl phosphate, thymidine 3′-p-nitrophenyl phosphate, and thymidine 5′-p-nitrophenyl phosphate. The latter compound was hydrolyzed at a very low rate. It did not hydrolyze adenosine 2′- or 5′- benzyl phosphate or certain nucleoside cyclic phosphates. The enzyme was inhibited by monoiodoacetate but not by heparin.

LINGCOD MUSCLE PHOSPHOMONOESTERASES: I. ACID PHOSPHATASES THAT HYDROLYZEp-NITROPHENYL PHOSPHATE

1960 ◽  
Vol 38 (1) ◽  
pp. 605-612 ◽  
Author(s):  
Neil Tomlinson ◽  
R. A. J. Warren
Keyword(s):  
Metal Ions ◽  
The Other ◽  
Acid Phosphatases ◽  
Free Base ◽  
Ph Optimum ◽  
Ophiodon Elongatus ◽  
Nitrophenyl Phosphate ◽  
Diethylaminoethyl Cellulose ◽  
Ph Range ◽  
Acid Phosphomonoesterase

Five fractions (A to E), each possessing acid phosphomonoesterase activity, were separated from an aqueous extract of the muscle of lingcod (Ophiodon elongatus) by stepwise chromatography on diethylaminoethyl cellulose in the free-base form.Fraction A required Zn++or Mn++for activity, was inhibited by heparin, and had its pH optimum at 6.0. Fraction E required Zn++for activity, was not inhibited by heparin, and had its pH optimum at 5.5. Fractions B, C, and D did not require metal ions for activity, and were distinguished from each other by differences in response to pH, cysteine, ethylenediaminetetraacetate, fluoride, and tartrate.The pH range over which fraction A was active was shifted to slightly higher values when Mn++was the activator rather than Zn++. Also, A was inhibited strongly by cysteine when activated by Zn++, but not when activated by Mn++. Data are presented that indicate these differences were due to different properties of the activating ions, rather than to the presence in fraction A of two enzymes, one activated by Zn++and the other by Mn++.

A study of the ribonucleic acid of normal and chloromycetin-inhibited bacteria by zone electrophoresis

1957 ◽  
Vol 23 ◽  
pp. 162-173 ◽  
Author(s):  
Arthur B. Pardee ◽  
Kenneth Paigen ◽  
Louise S. Prestidge
Keyword(s):  
Ribonucleic Acid ◽  
Zone Electrophoresis

scholarly journals Transfer ribonucleic acid methylases of bone. Studies on vitamin A and D deficiency

1972 ◽  
Vol 126 (5) ◽  
pp. 1057-1066 ◽  
Author(s):  
David S. Bradford ◽  
Bruce Hacker ◽  
Irwin Clark
Keyword(s):  
Vitamin D ◽  
Vitamin A ◽  
Ribonucleic Acid ◽  
Ribonuclease Activity ◽  
Supernatant Fraction ◽  
Mammalian Tissues ◽  
Biochemical Action ◽  
Rat Bone

Methods were devised for the assay of tRNA methylases of rat bone. The activities of bone tRNA methylases are similar to those from other mammalian tissues. However, unlike reports on liver methylases, no inhibitors were found in the supernatant fraction from pH5 precipitate of bone extracts. The effects of vitamins A and D on the methylation of tRNA by cell-free extracts of rat bone were studied. Deficiency of either vitamin resulted in a decrease in the rate and extent of tRNA methylation, whereas the administration of vitamin A to hypovitaminotic-A rats and vitamin D to hypovitaminotic-D rats increased the rate and extent of tRNA methylation. These effects appear to be apart from changes in ribonuclease activity or in concentrations of calcium or magnesium. No evidence of inhibitors of tRNA methylases was found in bone extracts from vitamin-deficient rats nor of activators in bone extracts from deficient rats given vitamin A or D. The pattern of tRNA methylation under conditions of vitamin A or D deficiency was not changed, suggesting a generalized cellular deficiency. It was of significance to find that the specificity for methylation of specific bases in tRNA was different after the administration of vitamin A as contrasted with the effects of vitamin D. The possible significance of tRNA methylation to the biochemical action of the vitamins on bone is discussed.

Interaction of Free Fatty Acids with Fish Muscle in Vitro

1974 ◽  
Vol 31 (1) ◽  
pp. 111-113 ◽  
Author(s):  
E. A. Childs
Keyword(s):  
Fatty Acids ◽  
Free Fatty Acids ◽  
Gel Electrophoresis ◽  
Fish Muscle ◽  
Safflower Oil ◽  
Fresh Fish ◽  
Ophiodon Elongatus

When fresh fish muscle (Ophiodon elongatus) was exposed to free fatty acids (safflower oil hydrolysate), the whole myofibril lost its suspensibility more readily than its component proteins lost their solubility. SDS-acrylamide gel electrophoresis indicated that tropomyosin was the most readily insolubilized protein. In the presence of 0.04% formaldehyde, effects of the free fatty acids were increased approximately threefold.

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