Multiple forms of brain adenylate cyclase: Stimulation by Mn2+

Daniel F. Malamuda; Concetta C. DiRusso; June R. Aprille

doi:10.1016/0005-2744(77)90211-X

Multiple forms of brain adenylate cyclase: Stimulation by Mn²⁺

Daniel F. Malamuda, Concetta C. DiRusso, June R. Aprille

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

Mn²⁺-stimulated adenylate cyclase (ATP pyrophosphate-lyase-(cyclizing), EC 4.6.1.1) activity in detergent solubilized preparations from mouse brain. While NaF-stimulated activity was decreased by both solubilization and storage at 0-4°C, the ability of the enzyme to be stimulated by Mn²⁺ was maintained for up to one week. By including Mn⁺ in the assay of adenylate cyclase in gel fractions after isoelectric focusing, two distinct peaks of enzyme activity (pI₁ = 5.8, pI₂ = 6.4) were detected, suggesting the existence of more than one type of catalytic subunit in mouse brain cell membranes.

Original language	English (US)
Pages (from-to)	243-247
Number of pages	5
Journal	BBA - Enzymology
Volume	485
Issue number	1
DOIs	https://doi.org/10.1016/0005-2744(77)90211-X
State	Published - Nov 23 1977
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

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@article{1b348398b5274fdb91680f9229990aed,

title = "Multiple forms of brain adenylate cyclase: Stimulation by Mn2+",

abstract = "Mn2+-stimulated adenylate cyclase (ATP pyrophosphate-lyase-(cyclizing), EC 4.6.1.1) activity in detergent solubilized preparations from mouse brain. While NaF-stimulated activity was decreased by both solubilization and storage at 0-4°C, the ability of the enzyme to be stimulated by Mn2+ was maintained for up to one week. By including Mn+ in the assay of adenylate cyclase in gel fractions after isoelectric focusing, two distinct peaks of enzyme activity (pI1 = 5.8, pI2 = 6.4) were detected, suggesting the existence of more than one type of catalytic subunit in mouse brain cell membranes.",

author = "Malamuda, {Daniel F.} and DiRusso, {Concetta C.} and Aprille, {June R.}",

note = "Funding Information: This work was supported by NIH GM 21700 and HD 08600, and NITHI 76-8-15-20. D.F.M. holds an NIH Career Development Award. The collaboration of Mr. T.C. Bell is gratefully acknowledged. We thank Dr. K.G. Walton for originally suggesting the use of Mn 2+ as a stimulatory agent.",

year = "1977",

month = nov,

day = "23",

doi = "10.1016/0005-2744(77)90211-X",

language = "English (US)",

volume = "485",

pages = "243--247",

journal = "BBA - Enzymology",

issn = "0005-2744",

publisher = "Elsevier BV",

number = "1",

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TY - JOUR

T1 - Multiple forms of brain adenylate cyclase

T2 - Stimulation by Mn2+

AU - Malamuda, Daniel F.

AU - DiRusso, Concetta C.

AU - Aprille, June R.

N1 - Funding Information: This work was supported by NIH GM 21700 and HD 08600, and NITHI 76-8-15-20. D.F.M. holds an NIH Career Development Award. The collaboration of Mr. T.C. Bell is gratefully acknowledged. We thank Dr. K.G. Walton for originally suggesting the use of Mn 2+ as a stimulatory agent.

PY - 1977/11/23

Y1 - 1977/11/23

N2 - Mn2+-stimulated adenylate cyclase (ATP pyrophosphate-lyase-(cyclizing), EC 4.6.1.1) activity in detergent solubilized preparations from mouse brain. While NaF-stimulated activity was decreased by both solubilization and storage at 0-4°C, the ability of the enzyme to be stimulated by Mn2+ was maintained for up to one week. By including Mn+ in the assay of adenylate cyclase in gel fractions after isoelectric focusing, two distinct peaks of enzyme activity (pI1 = 5.8, pI2 = 6.4) were detected, suggesting the existence of more than one type of catalytic subunit in mouse brain cell membranes.

AB - Mn2+-stimulated adenylate cyclase (ATP pyrophosphate-lyase-(cyclizing), EC 4.6.1.1) activity in detergent solubilized preparations from mouse brain. While NaF-stimulated activity was decreased by both solubilization and storage at 0-4°C, the ability of the enzyme to be stimulated by Mn2+ was maintained for up to one week. By including Mn+ in the assay of adenylate cyclase in gel fractions after isoelectric focusing, two distinct peaks of enzyme activity (pI1 = 5.8, pI2 = 6.4) were detected, suggesting the existence of more than one type of catalytic subunit in mouse brain cell membranes.

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