A microsomal iron-porphyrin activator of rat liver tryptophan pyrrolase.
نویسندگان
چکیده
Tryptophan pyrrolase, the enzyme that catalyzes the oxidation of tryptophan to formylkynurenine, has been localized in the 11,000 X g supernatant fraction of mammalian liver homogenates (l), which contains microsomes and cell sap. In the course of the present investigations (Z), it was observed that the isolated microsomal fraction of rat liver is devoid of this enzyme. However, addition of this microsomal fraction was found to stimulate the tryptophan pyrrolase activity of cell sap of rat liver homogenates. Studies on the nature of this activation suggest that the activating principle of microsomes is ferriprotoporphyrin, which may be serving as the prosthetic group of tryptophan pyrrolase.
منابع مشابه
The effects of chemical porphyrogens and drugs on the activity of rat liver tryptophan pyrrolase.
1. Drugs such as phenobarbitone and phenylbutazone, which increase the concentration of microsomal haem and cytochrome P-450, also increase the saturation of rat liver apo-(tryptophan pyrrolase) with its haem activator, as does the haem precursor 5-aminolaevulinate. 2. At 4h after the administration of the porphyrogens 2-allyl-2-isopropylacetamide, 3,5-diethoxycarbonyl-1,4-dihydrocollidine and ...
متن کاملThe activation and induction of rat liver tryptophan pyrrolase in vivo by its substrate.
Parenteral administration of tryptophan has been shown to increase markedly rat liver tryptophan pyrrolase activity (1). This phenomenon is often referred to as induction or adaptation due to its similarity to substrate-induced enzyme formation in microorganisms. The preceding article (2) documents the presence of a factor in microsomes which activates tryptophan pyrrolase of normal liver cell ...
متن کاملEffect of cytoplasmic particles on tryptophan pyrrolase activity of rat liver.
An activation of tryptophan pyrrolase in vitro distinct from the previously known conversion of inactive apotryptophan pyrrolase to active holotryptophan pyrrolase by hematin or by boiled particulate fractions of liver is described. This stimulation occurs by the addition of small amounts of mitochondria or microsomes to cell sap in the presence of excess methemoglobin. The particulate activato...
متن کاملPossible involvement of the enhanced tryptophan pyrrolase activity in the corticosterone- and starvation-induced increases in concentrations of nicotinamide-adenine dinucleotides (phosphates) in rat liver.
1. Deoxycorticosterone, which does not enhance tryptophan pyrrolase activity, also fails to alter the concentrations of the NAD(P) couples in livers of fed rats, whereas corticosterone increases both pyrrolase activity and dinucleotide concentrations. 2. Starvation of rats increases serum corticosterone concentration, lipolysis, tryptophan availability to the liver, tryptophan pyrrolase activit...
متن کاملThe nature and mechanism of the tryptophan pyrrolase (peroxidase-oxidase) reaction of Pseudomonas and of rat liver.
The oxidation reaction was catalyzed by an enzyme that had the following properties: (a) utilization of one molecule of oxygen in a single step, (b) inhibition by catalase, and (c) specific reversal of catalase inhibition by hydrogen peroxide from a donor reaction. Other properties of the enzyme, including cyanide and light reversible CO inhibitions, suggested that it was an iron porphyrin enzy...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 236 شماره
صفحات -
تاریخ انتشار 1961