Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation

Biochemistry ◽  
1980 ◽  
Vol 19 (16) ◽  
pp. 3656-3661 ◽  
Author(s):  
Neal C. Robinson ◽  
Fredlein Strey ◽  
Linda Talbert
Keyword(s):  
Boundary Layer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Triton X

Optimum pH and ionic strength for the assay of cytochrome c oxidase from pea cotyledon mitochondria

1977 ◽  
Vol 55 (10) ◽  
pp. 1114-1117 ◽  
Author(s):  
Gerrit H. Bomhoff ◽  
Mary Spencer
Keyword(s):  
Ionic Strength ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Ferrocytochrome C ◽  
Optimum Ph ◽  
Triton X ◽  
Assay Conditions ◽  
Nonionic Detergents

Cytochrome c oxidase (EC 1.9.3.1) has been solubilized by use of the nonionic detergents Triton X-114 and Triton X-100, from pea cotyledon mitochondria. Optimum assay conditions were determined for the oxidation of ferrocytochrome c in air. The results indicate that the plant cytochrome c oxidase resembles mammalian preparations in its sensitivity towards ionic strength and pH of the assay buffer.

Triton-X-100 induced dissociation of beef heart cytochrome c oxidase into monomers

Biochemistry ◽  
1986 ◽  
Vol 25 (9) ◽  
pp. 2328-2335 ◽  
Author(s):  
Neal C. Robinson ◽  
Linda Talbert
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart ◽  
Triton X

scholarly journals Canine submandibular-gland hyaluronidase. Identification and subcellular distribution

1968 ◽  
Vol 110 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Y. H. Tan ◽  
J. M. Bowness
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Submandibular Gland ◽  
High Speed ◽  
Specific Activity ◽  
Mitochondrial Fraction ◽  
Product Formation ◽  
Triton X ◽  
Submandibular Saliva ◽  
Testicular Hyaluronidase

1. Submandibular glands from four species of mammal have been shown to contain a hyaluronidase active at acid pH; glands from dog and cat had a much higher content of this enzyme than has been found in other sources. 2. Product formation from hyaluronate after 24hr. incubation was almost the same as with testicular hyaluronidase, indicating that the enzyme is an endo-poly-β-hexosaminidase. 3. When submandibular-gland homogenates were fractionated by the scheme developed for liver by de Duve, Pressman, Gianetto, Wattiaux & Appelmans (1955), all the enzymes assayed, except cytochrome c oxidase, were found to occur partly in the soluble fraction and partly in the particulate fractions. Among the particular fractions, the highest specific activity was found in the heavy-mitochondrial fraction for cytochrome c oxidase, in the microsomal fraction for alkaline phosphatase and in the light-mitochondrial fraction for acid phosphatase, β-N-acetylhexosaminidase and acid-active hyaluronidase. 4. Release of the enzyme activity from the sedimentable fractions occurred in 0·1% Triton X-100 or after high-speed homogenization. 5. Stimulation of dogs by pilocarpine was found to decrease the hyaluronidase content of the submandibular gland by 5% and to cause the occurrence of a corresponding amount of acid-active hyaluronidase in the submandibular saliva. 6. The results are discussed in relation to the subcellular localization of hyaluronidase.

Mechanism of Inhibition of Cytochrome c Oxidase by Triton X-100

2021 ◽  
Vol 86 (1) ◽  
pp. 44-58
Author(s):  
Ilya P. Oleynikov ◽  
Natalia V. Azarkina ◽  
Tatiana V. Vygodina ◽  
Alexander A. Konstantinov
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mechanism Of Inhibition ◽  
Triton X
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