Purification and Properties of δ-Aminolevulinate Dehydratase from Tissues of Two Strains of Mice

Dl, Coleman

doi:10.1016/s0021-9258(18)96372-6

Cited by 74 publications

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“…The tobacco-leaf enzyme appeared more temperaturesensitive than that from yeast or cow liver. Energy of activation for the tobacco-leaf enzyme was somewhat lower than that reported for the enzyme from mouse (Coleman, 1966).…”

contrasting

confidence: 58%

“…Whereas 8-aminolaevulate dehydratase is generally known to behave like a typical thiol enzyme, the effect of EDTA and various cations on the enzyme appears to differ with enzyme sources. Activation by EDTA was observed in preparations from mice (Coleman, 1966), but inhibition was noted in certain other preparations (Gibson, 1955;Gibson, Neuberger & Scott, 1955;Batlle, Ferramola & Grinstein, 1967;DeBarreiro, 1967). Nandi & Waygood (1967) reported that the inhibition by EDTA of the enzyme from wheat leaves was reversed by addition ofMn2+.…”

mentioning

confidence: 99%

“…Burnham & Lascelles (1963) observed no inhibition by EDTA of the enzyme from Rhodopseudomonas spheroides. Fe2+ was reported to activate the enzyme from mice (Coleman, 1966), but to inhibit that from ox liver (Gibson et al 1955). Nandi & Waygood (1967) reported neither an activation nor an inhibition of wheat-leaf enzyme by 10nm-Fe2+.…”

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confidence: 99%

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Purification and general properties of δ-aminolaevulate dehydratase from Nicotiana tabacum L.

Shetty

Miller

1969

Biochemical Journal

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1. delta-Aminolaevulate dehydratase (EC 4.2.1.24) was purified 80-fold from tobacco leaves and its properties were studied. 2. The enzyme had optimum pH7.4 in potassium phosphate buffer, K(m)6.25x10(-4)m at 37 degrees and pH7.4, optimum temperature 45 degrees and an activation energy of 11100 cal./mole. 3. The enzyme lost activity when prepared in the absence of cysteine, and this activity was only partly restored by the later addition of thiols. Reagents for thiol groups inactivated the enzyme. 4. Mg(2+) was essential for activity, and EDTA and Fe(2+) were inhibitory; Mn(2+) was an activator or an inhibitor depending on the concentration.

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Purification and general properties of δ-aminolaevulate dehydratase from Nicotiana tabacum L.

Shetty

Miller

1969

Biochemical Journal

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“…(Neuberger 1955, Calissano καί συν. 1966) μέ έ£αίρεσιν τό ενζυμον τό όποιον προέρχεται έκ τοϋ μυός (Coleman, 1966) . 'Επίσης ή αίμίνη καί ή πρωτοπορφυρίνη αναστέλλουν τήν δ-ALA ϋμέέπίτασιν επί απουσίας καλίου (Κ) , όπως παρετηρήθη είς τάς ερ γασίας τών Coleman 1966, Calissano καί συν.…”

Section: ετεροζυγος μεσογειακη αναιμιαunclassified

“…1966) μέ έ£αίρεσιν τό ενζυμον τό όποιον προέρχεται έκ τοϋ μυός (Coleman, 1966) . 'Επίσης ή αίμίνη καί ή πρωτοπορφυρίνη αναστέλλουν τήν δ-ALA ϋμέέπίτασιν επί απουσίας καλίου (Κ) , όπως παρετηρήθη είς τάς ερ γασίας τών Coleman 1966, Calissano καί συν. 1966 Τά υπόλοιπα ένζυμικά στάδια συνθέσεως αϊμης δέν έ χουν τύχει μέχρι τοϋδε μελέτης κεχωρισμένως πλην τοϋ στα δίου τοϋ πολυμερισμοϋ τοϋ μονοπυρρολίου πορφοχολινογόνου προς τό πρώτον τετραπυρρόλιον της σειράς δηλαδή τοϋ ούροπορφυρινογόνου, τό όποιον προσφάτως έμελετήθη ύπό τοϋ An derson καί συν.…”

Section: ετεροζυγος μεσογειακη αναιμιαunclassified

Η Δραστηριοτης Του Ενζυμου Συνθεταση Ουροπορφυρινογονου Ι Των Ερυθρο- Κυτταρων Επι Ετεροζυγου -Β- Μεσογειακης Αναιμιας

Λαζανασ¹

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Acute effects of orally administered sodium arsenate on heme biosynthetic enzymes in the tissues of three strains of mice

Kondo

Ichikawa

1999

Appl. Organometal. Chem.

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Sodium arsenate (Na2HASO4· 7H2O, As(V)) was administered to three genetically different strains of mice, ICR, C57BL/6J and DBA/2J, in a single oral dose of 54 mg kg−1 body weight. The effects on the activities of heme biosynthetic enzymes in the spleen, liver, kidney and peripheral blood were investigated. The activities of δ‐aminolevulinate synthase (ALAS, EC 2.3.1.37), catalyzing the first reaction in the heme biosynthetic pathway and the rate‐limiting enzyme for heme synthesis, δ‐aminolevuilinate dehydratase (ALAD, EC 4.2.1.24) and porphobilinogen de‐aminase (PBGD, EC 4.3.1.8) in the spleens of the ICR strain, were remarkably reduced to 51%, 32% and 42%, respectively, in comparison with each mean value of the control group. In contrast, these activities were significantly increased in the livers of the C57BL/6J strain, and a similar trend was observed in the DBA/2J strain. In the kidneys, the ALAD activity was significantly reduced in the ICR strain, but no significant differences in the other two strains were found. These results suggest that the influence of As(V) on the activity of heme biosynthetic enzymes is most potently manifested in the spleen tissue of the ICR strain. Copyright© 1999 John Wiley & Sons, Ltd.

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Purification and Properties of δ-Aminolevulinate Dehydratase from Tissues of Two Strains of Mice

Cited by 74 publications

References 10 publications

Purification and general properties of δ-aminolaevulate dehydratase from Nicotiana tabacum L.

Purification and general properties of δ-aminolaevulate dehydratase from Nicotiana tabacum L.

Η Δραστηριοτης Του Ενζυμου Συνθεταση Ουροπορφυρινογονου Ι Των Ερυθρο- Κυτταρων Επι Ετεροζυγου -Β- Μεσογειακης Αναιμιας

Acute effects of orally administered sodium arsenate on heme biosynthetic enzymes in the tissues of three strains of mice

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