By B. Connor Johnson
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Additional info for Posttranslational Covalent Modifications of Proteins
Sample text
1970)· S i n c e insulin i n s u l i n was was et Since k n o w n to t o decrease d e c r e a s e cAMP levels l e v e l s in i n adipose a d i p o s e ttissue i s s u e and a n d liver liver known t h a t had had p r e v i o u s l y been b e e n elevated elevated b a d r e n a l i n and a n d glucagon glucagon that previously byy adrenalin r e s p e c t i v e l y , an a n obvious o b v i o u s possibility p o s s i b i l i t y was w a s that t h a t insulin i n s u l i n actiacti respectively, v a t e d muscle m u s c l e glycogen g l y c o g e n synthase s y n t h a s e by b y the t h e same s a m e mechanism, m e c h a n i s m , rere vated s u l t i n g in i n decreased d e c r e a s e d cAMP-PrK c A M P - P r K activity.
The data are details are given in legend to IV. The data are taken from Parker e t ale a l . [1982b]. [1982b]. taken from Parker et Μ ΙΟ •μ Q) 0) ΓΙ 0 •Υ q Q) 0 4J Υ 0) ΊΟ Οι TO 0 Α, Λ: q TO TO 0) 0) •Η •μ Η & 0 ϋ Α, •Η q •Ρ •Η Q) 4J q q Α Μ TO fO -Ρ rq 8φ Η CJ Q) q CD 0 CO CD bl Υ 3ι Ή Μ Ϋ 3 CO *! 0 q ΰι •ρ CO ΜΗ ΜΗ • Η TABLE IV. Effect of Insulin on the Kinetic Properties and Phosphate Content of Sk Skeletal Muscle Glycogen synthasea,b +J Q) Ή q •P ~>- q -P Ρ ^ O 3 CD 4J 5§ q 3 CO 6 Ν - Μ r> § Β — I CO Ή !
T w o enzymes enzymes Two t e r m e d protein p r o t e i n phosphatase-1 phosphatase-1 ( P r P - 1 ) and and p h o s p h a t a s e 2A 2 A ((PrPPrPtermed (PrP-1) phosphatase 2 A ) are a r e capable c a p a b l e of o f dephosphorylating d e p h o s p h o r y l a t i n g sites sites ( 3 a + 3 b + 3 c ) in in 2A) (3a+3b+3c) vitro, v i t r o , PrP-1 PrP-1 b being e i n g the t h e dominant d o m i n a n t activity a c t i v i t y (section ( s e c t i o n 3). 3). HowHow ever, (3a+3b+ e v e r , neither n e i t h e r enzyme e n z y m e is i s specific s p e c i f i c for f o r sites sites ( 3 a + 3 b + 3c), 3 c ) , and and site-2 s i t e - 2 is i s dephosphorylated d e p h o s p h o r y l a t e d with w i t h almost a l m o s t equal e q u a l rapidity r a p i d i t y in in vitro 1982).