scholarly journals INTRACELLULAR LOCALIZATION OF ENZYMES IN SPLEEN

1962 ◽  
Vol 12 (2) ◽  
pp. 263-276 ◽  
Author(s):  
Herbert J. Eichel ◽  
Jay S. Roth

Some properties of rat spleen ribonuclease have been studied, and the intracellular distribution of the enzyme and ribonucleic acid have been presented. Spleen ribonuclease exhibits maximal activity at pH 5.8, and although there is some evidence for the presence of an enzyme with an optimum at pH 7.0, it is not conclusive. The enzyme is concentrated primarily in the mitochondrial fraction, but significant quantities occur in the supernatant fluid. The latter contains ribonuclease inhibitor similar to that found in liver. The effects of whole body x-irradiation, magnesium ion, substrate concentration, type of buffer, presence of p-chloromercuriphenylsulfonic acid, deoxycholate, and Triton X-100 on ribonuclease activity are examined.

1973 ◽  
Vol 55 (2) ◽  
pp. 304 ◽  
Author(s):  
A. Ferencz ◽  
E. J. Hidvégi ◽  
L. D. Szabó ◽  
V. Várterész ◽  
E. J. Hidvegi ◽  
...  

1970 ◽  
Vol 42 (3) ◽  
pp. 560 ◽  
Author(s):  
L. Ababei ◽  
C. Haler ◽  
M. Trandafirescu ◽  
D. Cernătescu ◽  
M. Ionescu ◽  
...  

1977 ◽  
Vol 75 (1) ◽  
pp. 135-147 ◽  
Author(s):  
A L Blitz ◽  
R E Fine ◽  
P A Toselli

Coated vesicles from the brain have been purified to near morphological homogeneity by a modification of the method of Pearse. These vesicles resemble sarcoplasmic reticulum fragments isolated from skeletal muscle. They contain proteins with 100,000- and 55,000-dalton mol wt which co-migrate on polyacrylamide gels, in the presence of sodium dodecyl sulfate, with the two major proteins of the sarcoplasmic reticulum fragment. These vesicles contain adenosine triphosphatase (ATPase) activity which is stimulated by calcium ions in the presence of Triton X-100 (Rohm & Haas Co., Philadelphia, Pa.), displaying maximal activity at 8 x 10(-7) M Ca ++. They take up calcium ions from the medium, and this uptake is stimulated by ATP and by potassium oxalate, a calcium-trapping agent. The 100,000-dalton protein of the coated vesicles displays immunological reactivity with an antiserum directed against the 100,000-dalton, calcium-stimulated ATPase of the sarcoplasmic reticulum. As with the sarcoplasmic reticulum fragment, this protein becomes radiolabeled when coated vesicles are briefly incubated with gamma-labeled [32P]ATP. The possible functions of coated vesicles as calcium-sequestering organelles are discussed.


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