TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 270, No. 30, Issue of July 28, pp. 17970-17976, 1995 Printed in U.S.A. Hydrophobicity and Subunit Interactions of Rod Outer Segment Proteins Investigated Using Triton X-114 Phase Partitioning* (Received for publication, November 14, 1994, and in revised form, April 14, 1995) John M. Justice:j:, James J. Murtagh, Jr.§, Joel Moss, and Martha Vaughan From the Pulmonary-Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 the presence of receptor, G ,, and effector (4-7). Triton X-114 phase partitioning, a procedure used for purifying integral membrane proteins, was used to Domains ofG" involved in interaction with receptor and G 'Y study protein components of the mammalian visual have been mapped using a variety of methods. It was concluded transduction cascade. An integral membrane protein, that the amino-terminal region of Gta is important for its in­ rhodopsin, and two isoprenylated protein complexes, teraction with G 'Y. Removal of the first 18 amino acids from the cyclic GMP phosphodiesterase and Gtti'Y' partitioned amino terminus of Gta by trypsin abolished Gtf3y stimulation of into the detergent-rich phase. Arrestin, a soluble pro­ pertussis toxin-catalyzed ADP-ribosylation, although the ADP­ tein, accumulated in the aqueous phase. Gta distributed 
TI - Hydrophobicity and Subunit Interactions of Rod Outer Segment Proteins Investigated Using Triton X-114 Phase Partitioning
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.270.30.17970
DA - 1995-07-01
UR - https://www.deepdyve.com/lp/unpaywall/hydrophobicity-and-subunit-interactions-of-rod-outer-segment-proteins-H005j0MFSE
DP - DeepDyve
ER -