STUDIES ON RESPIRATORY ENZYMES OF ADRENAL GLAND .1. MEDULLA

  • 1 January 1961
    • journal article
    • research article
    • Vol. 236  (1) , 225-+
Abstract
The predominant cytochrome of the adrenal medulla is a compound showing an absorption band at 559 m[mu] upon reduction with cysteine, adrenaline, ascorbate, and reduced diphospho- and reduced triphospho-pyridine nucleotide. Upon differential centrifugation of homogenates of the tissue, this hemochromogen is found in a microsomal fraction and in the granules rich in catechol amines. A clean separation of mitochondria and the granules containing catechol amines could not be achieved. A fraction was obtained however, in which an enrichment of cytochrome b + cytochromes a+a3 could be demonstrated spectro-scopically. Cytochrome c in the whole medulla was extracted and determined quantitatively. Its content is only 8% of that found in beef heart. The quantitative distribution of the enzymes succinate dehydrogenase, reduced diphospho- and reduced triphosphopyridine nucleotide cytochrome c reductase, and transhydrogenase in the various fractions of the medulla has been measured. It was found that the content of enzymes in the medulla capable of gearing electron transport from reduced triphosphopyridine nucleotide to oxygen was greatly exceeded by the values reported in the literature for its content of enzymes capable of producing reduced triphosphopyridine nucleotide. This relationship is discussed in regard to the use of reduced triphosphopyridine nucleotide by the gland for reductive synthetic purposes.

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