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At least 793 records · Page 44Linked to original sources
PubMed1978

[Porphobilinogen biosynthesis from delta-aminolevulinic acid by the internal organs of white rats].

The capacity for porphobilinogen (PBG) biosynthesis from aminolevulinic acid (ALA) in the homogenates of the lung, heart, liver, kidney, pancreatic and small intestinal tissues of 77 albino rats was determined, and all the mentioned organs were found to be capable of PBG biosynthesis. The greatest ALA dehydratase activity was found in the tissue of the liver, then -- in the order of decreasing activity -- in the tissues of the kidneys, lungs, pancreas, small intestine, heart and spleen. On addition of lead solution to the synthesizing system a significant reduction in the activity of the enzyme was revealed in the tissue of the liver; the activity was unchanged in the kidney tissue. No changes in the toxic effect of lead were found on simultaneous addition of lead and D-penicillamine.

Aminolevulinic Acid↗
PubMed1990

Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a delta-aminolevulinic acid-dependent mutant strain.

The Rhodobacter capsulatus hemA gene, coding for the enzyme delta-aminolevulinic acid synthase (ALAS), was isolated from a genome bank by hybridization with a hemT probe from Rhodobacter sphaeroides. Subcloning of the initial 3.9 kb HindIII fragment allowed the isolation of a 2.5 kb HindIII-BglII fragment which was able to complement the delta-aminolevulinic acid-requiring (ALA-requiring) Escherichia coli mutant SHSP19. DNA sequencing revealed an open reading frame coding for a protein with 401 amino acids which displayed similarity to the amino acid sequences of other known ALASs. However, no resemblance was seen to the HemA protein of E. coli K12. Based on the sequence data, an ALA-requiring mutant strain of R. capsulatus was constructed by site-directed insertion mutagenesis. Introduction of a plasmid, containing the hemA gene of R. capsulatus on the 3.9 kb HindIII fragment, restored ALA-independent growth of the mutant indicating that there is only one gene for ALA biosynthesis in R. capsulatus. Transfer of the R' factor pRPS404 and hybridization analysis revealed that the ALAS gene is not located within the major photosynthetic gene cluster.

5-Aminolevulinate Synthetase↗
PubMed1987

Evaluation of a new specific analysis of urinary delta-aminolevulinic acid in man.

A new specific method for urinary delta-aminolevulinic acid (ALA-U) measurement in man as a serial screening method for health control in occupational lead exposure was compared with a recommended, selective test (DAVIS method). The new test can be run fully automated, and the cost of material per sample is much lower than in the DAVIS method. ALA values obtained with this specific method were lower than those measured with the DAVIS method (= DAVIS values) in each case due to the elimination of interfering urinary compounds. In DAVIS values below the biological tolerance level (BAT-level) of 15 mg/l, the percentage of interfering compounds varied between 10 and 80%; above BAT level, these components represented about 20% of the total amount of ALA-U. A strong correlation can be demonstrated between specifically measured ALA values and the enzyme activity of ALA-dehydratase (ALA-D) in blood at lead levels (Pb-B) below 35 micrograms/dl (r = -0.768 for ALA-U/log ALA-D; n = 18).

Aminolevulinic Acid↗
PubMed1987

In vitro distribution of porphyrin metabolites from 10(-3) M delta-aminolevulinic acid in primary neural tissue cultures.

The distribution of porphyrin metabolites (uro-7-6-5-copro-3-proto-heme) from 10(-3) M delta-aminolevulinic acid (ALA) in neuronal and glial primary cultures was examined by an isotopic technique. In both cell types, 8-9% of the total production (cell + medium) was found in the cells and more than 90% in the medium. In both the cells and the medium the predominant porphyrin fraction was uro + 7 carboxylic. The heme fraction of the cells was also very high. Through the exclusion of ALA-synthetase activity, the "Uroporphyria-like-model" of "hepatic porphyria" was demonstrated.

Aminolevulinic Acid↗
PubMed1989

Free radical generation during delta-aminolevulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies.

delta-Aminolevulinic acid (ALA), a heme precursor accumulated in acute intermittent porphyria and saturnism, undergoes autoxidation leading to ammonium ion and probably the corresponding alpha-ketoaldehyde. This reaction is accelerated by addition of oxyhemoglobin (oxyHb) and other iron complexes. OxyHb is concomitantly oxidized to metHb; the apparent second-order rate constant of oxyHb/ALA coupled oxidation is ca. 10 M-1 min-1.1H NMR and uv spectral studies suggest that ALA undergoes enolization before consuming the dissolved oxygen. Spin-trapping experiments demonstrate formation of both the hydroxyl radical and a substrate-derived carbon-centered radical during ALA oxidation. Generation of active oxygen species by ALA might be related to the neuropathy associated to some acquired and inherited porphyrinpathies.

Aminolevulinic Acid↗
PubMed1979

Formation of delta-aminolevulinic acid from glutamic acid by a partially purified enzymes system from wheat leaves.

A method for partial purification of an enzyme system from greening wheat leaves which converts 14C-labeled glutamate to delta-aminolevulinic acid is described. The purification entails the successive use of anion and cation exchange, followed by molecular sieving. The enzyme system is unstable in crude form, but the stability is markedly increased after column chromatography on CM-cellulose. The pH profile and the cofactor requirements suggest that at least two enzymes are involved.

Aminolevulinic Acid↗