Chandrika, SR and Padmanaban, G (1980) Purification, properties and synthesis of delta-aminolaevulinate dehydratase from Neurospora crassa. In: Biochemical Journal, 191 (1). pp. 29-36.
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Delta-aminolaevulinate dehydratase, the second and rate-limiting enzyme of the haem-biosynthetic pathway, was purified 300-fold from induced cultures of Neurospora crassa. The native enzyme has a mol.wt. of about 350000, whereas the salt-treated enzyme after incubation at 37 degrees C for 10 min has a mol.wt. of about 232000. The mol.wt. of the subunit is about 38000. Antibodies to the purified enzyme were raised in rabbits. By using radiolabelling and immunoprecipitation techniques it was shown that addition of iron and laevulinate to iron-deficient cultures brings about a significant increase in the synthesis of the enzyme, and protoporphyrin, the penultimate end product of the pathway, represses enzyme synthesis.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to the Biochemical Society.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||08 Feb 2010 07:05|
|Last Modified:||19 Sep 2010 05:32|
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