نتایج جستجو برای: protoporphyrin ix

تعداد نتایج: 20130  

Journal: :Molecular and cellular biology 1992
E M Coccia V Profita G Fiorucci G Romeo E Affabris U Testa M W Hentze A Battistini

The mechanisms that regulate the expression of the H chain of the iron storage protein ferritin in Friend erythroleukemia cells (FLCs) after exposure to hemin (ferric protoporphyrin IX), protoporphyrin IX, and ferric ammonium citrate (FAC) have been investigated. Administration of hemin increases the steady-state level of ferritin mRNA about 10-fold and that of ferritin protein expression 20-fo...

2010
Brian Pogue Venkataramanan Krishnaswamy Frederic LeBlond Brian W. Pogue

A high frequency ultrasound-coupled fluorescence tomography system, which was primarily designed for imaging protoporphyrin IX production in skin tumors in vivo, is demonstrated for the first time. Protoporphyrin IX is an endogenous, fluorescent molecule produced naturally in the heme biosynthesis pathway, with enhanced production in many cancerous tumors. The design couples non-contact fiber-b...

Journal: :The Biochemical journal 2007
Artur Sawicki Robert D Willows

The enzyme BchM (S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase) from Rhodobacter capsulatus catalyses an intermediate reaction in the bacteriochlorophyll biosynthetic pathway. Overexpression of His(6)-tagged protein in Escherichia coli resulted in the majority of polypeptide existing as inclusion bodies. Purification from inclusion bodies was performed using metal-affi...

Journal: :The Biochemical journal 2001
R Franco A S Pereira P Tavares A Mangravita M J Barber I Moura G C Ferreira

Ferrochelatase (EC 4.99.1.1) is the terminal enzyme of the haem biosynthetic pathway and catalyses iron chelation into the protoporphyrin IX ring. Glutamate-287 (E287) of murine mature ferrochelatase is a conserved residue in all known sequences of ferrochelatase, is present at the active site of the enzyme, as inferred from the Bacillus subtilis ferrochelatase three-dimensional structure, and ...

Journal: :The Journal of biological chemistry 1946
E J CHU

Protoporphyrin IX dimethyl ester, a crystalline compound with a definite melting point, is generally used to identify protoporphyrin IX. Various methods of preparation (l-4) have been described in the literature. As indicated by Grinstein and Watson (5, S), application of chromatographic separation is necessary in order to obtain a pure product. By following the procedures thus far described in...

Journal: :The Journal of Cell Biology 1974
Wei-Yeh Wang Wenan Lee Wang John E. Boynton Nicholas W. Gillham

In this report we describe two nonallelic Mendelian protoporphyrin accumulating mutants br(s)-1 and br(c)-1. Results of experiments with these mutants lead us to postulate that porphyrin biosynthesis branches into light and dark steps between protoporphyrin-IX and magnesium protoporphyrin. We hypothesize that the br(c) locus controls a dark step while the br(s) locus either controls a step in t...

Journal: :Clinical chemistry 1980
G R Gotelli J H Wall P M Kabra L J Marton

We describe a method for simultaneously measuring concentrations of coproporphyrin, zinc protoporphyrin IX, and protoporphyrin IX in whole blood by liquid chromatography, with use of reversed-phase ion-pair system, fluorometric detection, and internal standardization. Each analysis requires 10 microL of whole blood and 15 min total analysis time. Analytical recovery ranged from 84 to 92%, day-t...

Journal: :Acta dermato-venereologica 1999
A M Wennberg F Gudmundson B Stenquist A Ternesten L Mölne A Rosén O Larko

Photodynamic therapy has become an interesting alternative to conventional therapy for basal cell carcinomas. Delta-aminolevulinic acid is a precursor in the biosynthesis of protoporphyrin IX that accumulates to a large extent in tumour tissue. We have compared in vivo protoporphyrin IX fluorescence with the extent of basal cell carcinomas on the face, trunk and thigh determined by histological...

2016
Charlie Hobbs Harry A. Dailey Mark Shepherd

Bacteria require a haem biosynthetic pathway for the assembly of a variety of protein complexes, including cytochromes, peroxidases, globins, and catalase. Haem is synthesised via a series of tetrapyrrole intermediates, including non-metallated porphyrins, such as protoporphyrin IX, which is well known to generate reactive oxygen species in the presence of light and oxygen. Staphylococcus aureu...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید