Differences in the structure of A and B forms of human monoamine oxidase

R. M. Cawthon, J. E. Pintar, F. P. Haseltine, X. O. Breakefield

Research output: Contribution to journalArticle

Abstract

[3H]Pargyline-labeled polypeptides associated with the A and B types of monoamine oxidase (MAO) activity in human tissues were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). [3H]Pargyline was bound to MAO A in a crude mitochondrial fractions from the placental trophoblast of a male newborn and to MAO B in blood platelets from the umbilical vein of the same newborn. [3H]Pargyline was also bound to MAO A and B in a crude mitochondrial fraction from cultured skin fibroblasts of a male adult and to MAO B in blood platelets from the same individual. Specific labeling of proteins associated with type A or type B activity in fibroblast cells was achieved by preincubation with selective B or A inhibitors, respectively. For all tissues, SDS-PAGE of [3H]pargyline-bound samples revealed a labeled protein band of apparent molecular weight 63,000 for MAO A and 60,000 for MAO B. When SDS-solubilized, [3H]pargyline-labeled MAO A and B proteins from the same male newborn were subjected to limited proteolysis and one-dimensional peptide mapping in SDS gels, different patterns of [3H][argyline-labeled peptides were obtained. these findings indicate that distinct enzyme molecules are associated with the A and B types of human MAO activity.

Original languageEnglish (US)
Pages (from-to)363-372
Number of pages10
JournalJournal of Neurochemistry
Volume37
Issue number2
StatePublished - 1981
Externally publishedYes

Fingerprint

Monoamine Oxidase
Pargyline
Fibroblasts
Platelets
Electrophoresis
Sodium Dodecyl Sulfate
Peptides
Blood
Polyacrylamide Gel Electrophoresis
Blood Platelets
Tissue
Proteolysis
Proteins
Umbilical Veins
Peptide Mapping
Trophoblasts
Labeling
Human Activities
Skin
Gels

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Cawthon, R. M., Pintar, J. E., Haseltine, F. P., & Breakefield, X. O. (1981). Differences in the structure of A and B forms of human monoamine oxidase. Journal of Neurochemistry, 37(2), 363-372.

Differences in the structure of A and B forms of human monoamine oxidase. / Cawthon, R. M.; Pintar, J. E.; Haseltine, F. P.; Breakefield, X. O.

In: Journal of Neurochemistry, Vol. 37, No. 2, 1981, p. 363-372.

Research output: Contribution to journalArticle

Cawthon, RM, Pintar, JE, Haseltine, FP & Breakefield, XO 1981, 'Differences in the structure of A and B forms of human monoamine oxidase', Journal of Neurochemistry, vol. 37, no. 2, pp. 363-372.
Cawthon RM, Pintar JE, Haseltine FP, Breakefield XO. Differences in the structure of A and B forms of human monoamine oxidase. Journal of Neurochemistry. 1981;37(2):363-372.
Cawthon, R. M. ; Pintar, J. E. ; Haseltine, F. P. ; Breakefield, X. O. / Differences in the structure of A and B forms of human monoamine oxidase. In: Journal of Neurochemistry. 1981 ; Vol. 37, No. 2. pp. 363-372.
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AB - [3H]Pargyline-labeled polypeptides associated with the A and B types of monoamine oxidase (MAO) activity in human tissues were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). [3H]Pargyline was bound to MAO A in a crude mitochondrial fractions from the placental trophoblast of a male newborn and to MAO B in blood platelets from the umbilical vein of the same newborn. [3H]Pargyline was also bound to MAO A and B in a crude mitochondrial fraction from cultured skin fibroblasts of a male adult and to MAO B in blood platelets from the same individual. Specific labeling of proteins associated with type A or type B activity in fibroblast cells was achieved by preincubation with selective B or A inhibitors, respectively. For all tissues, SDS-PAGE of [3H]pargyline-bound samples revealed a labeled protein band of apparent molecular weight 63,000 for MAO A and 60,000 for MAO B. When SDS-solubilized, [3H]pargyline-labeled MAO A and B proteins from the same male newborn were subjected to limited proteolysis and one-dimensional peptide mapping in SDS gels, different patterns of [3H][argyline-labeled peptides were obtained. these findings indicate that distinct enzyme molecules are associated with the A and B types of human MAO activity.

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