Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it.

Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Research Abstract Details 

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Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Abstract Text:

M Ando-Yamamoto,H Hayashi,T Sugiyama,H Fukui,T Watanabe,H Wada,

L-DOPA decarboxylase [DDC, aromatic-L-amino acid carboxyl-lyase, EC 4.1.1.28] was purified 800-fold from rat liver by several column chromatographic steps. The enzyme (specific activity, about 6 mumol/min X mg protein) had a molecular weight of 100,000 and gave a single band with a molecular weight of 50,000 on SDS-polyacrylamide gel electrophoresis. Its isoelectric point was pH 5.7. The absorption spectrum in the visible region of the purified DDC showed maxima at 330 and 420 nm. Polyclonal and monoclonal antibodies against DDC were produced by using this purified protein as an antigen. Polyclonal anti-DDC serum immunoprecipitated the DDC activities of rat, guinea-pig and rabbit livers (about 1, 10, and more than 100 microliter of antiserum, respectively, were required for 50% precipitation of 2 nmol/min of activity of these enzymes). The monoclonal antibody, named MA-1, belonged to the IgG1 subclass and immunoprecipitated the DDC activities of rat and guinea-pig livers to the same extent (about 0.5 micrograms of IgG was required to immunoprecipitate 2 nmol/min activity of each enzyme), but it did not affect the rabbit enzyme. The antibody MA-1 detected DDC molecules of both the purified enzyme and crude homogenate of rat liver blotted onto a nitrocellulose sheet. Immunohistochemically this antibody also stained specific neurons in the substantia nigra, raphe nucleus and locus coeruleus of rat brain.

Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Publishing Authors By Initials

M Ando-Yamamoto,H Hayashi,T Sugiyama,H Fukui,T Watanabe,H Wada,

For similar animals: animal population groups: animals, inbred strains: rats, inbred strains research abstracts see: animals: animal population groups: animals, inbred strains: rats, inbred strains research

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Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 101

Page Numbers: 405-14

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1987

Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Keywords Mesh Terms:

KEYWORDS: Rats, Inbred Strains

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it. Information

Substance Name: Aromatic-L-Amino-Acid Decarboxylases

Registry Number: EC 4.1.1.28

Grant and Affiliation Information for Purification of L-dopa decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it.

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Country: JAPAN

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MEDLINETA: J Biochem

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