TY - JOUR
T1 - Hormone-Sensitive Adenylate Cyclase
T2 - Identity, Function, and Regulation of the Protein Components
AU - Ross, Elliott M.
AU - Pedersen, Steen E.
AU - Florio, Vincent A.
N1 - Funding Information:
Studies from this laboratory cited here have been supported by USPHS grant GM30355. E. M. R. is an Established Investigator of the American Heart Association and V. A. F. is the recipient of a graduate fellowship from the Pharmaceutical Manufacturers‘ Association Foundation.
PY - 1983/1/1
Y1 - 1983/1/1
N2 - The hormone-sensitive adenylate cyclase system in the plasma membrane of target cells consists of at least three distinct protein species. This chapter discusses the approach to study this hormone-sensitive adenylate cyclase and proteins complex network by trying first to identify and separate these individual protein components, to study them in isolation using increasingly pure preparations, and then to study their interactions and regulation after suitable reconstitution. Results from the laboratory that stress the basic analytical approach to a multienzyme regulatory complex are described. It is assumed that all vertebrate, membrane bound, hormone-sensitive adenylate cyclases are qualitatively similar in their regulation and composition. Observed differences among different cells merely reflect differences in the concentration of each protein or quantitative differences in their kinetic or equilibrium constants rather than qualitative differences in mechanism. As adenylate cyclase components prepared from different cells are shown to be capable of interacting with each other, this assumption is increasingly supported.
AB - The hormone-sensitive adenylate cyclase system in the plasma membrane of target cells consists of at least three distinct protein species. This chapter discusses the approach to study this hormone-sensitive adenylate cyclase and proteins complex network by trying first to identify and separate these individual protein components, to study them in isolation using increasingly pure preparations, and then to study their interactions and regulation after suitable reconstitution. Results from the laboratory that stress the basic analytical approach to a multienzyme regulatory complex are described. It is assumed that all vertebrate, membrane bound, hormone-sensitive adenylate cyclases are qualitatively similar in their regulation and composition. Observed differences among different cells merely reflect differences in the concentration of each protein or quantitative differences in their kinetic or equilibrium constants rather than qualitative differences in mechanism. As adenylate cyclase components prepared from different cells are shown to be capable of interacting with each other, this assumption is increasingly supported.
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U2 - 10.1016/S0070-2161(08)60529-8
DO - 10.1016/S0070-2161(08)60529-8
M3 - Article
AN - SCOPUS:0005553833
SN - 0070-2161
VL - 18
SP - 109
EP - 142
JO - Current Topics in Membranes and Transport
JF - Current Topics in Membranes and Transport
IS - C
ER -