How to Write 8/100 as a Decimal?
Tessier D. A , red asterisks denote single, double, or triple contiguous alanine mutations that produced a loss of SRE-luciferase activity in both the absence and presence of cholesterol.
If you originally registered with a username please use that to sign in. In cells that received no Scap, there was little firefly luciferase activity Fig. C , competitive binding of unlabeled sterols to His 10 -Scap TM1—8. We therefore believe that cholesterol binding does not alter the tetrameric state.
We also considered the formal possibility that Scap YA was simply failing to fold properly and was retained in the ER through the unfolded protein response.
How to reduce (simplify) fraction 8/ to lowest terms? Calculator, explanations
You have entered an invalid code. Three of the loops Loops 1, 6, and 7 are long enough to have significant structure. It offers Voltage and Amps meters for effective system monitoring. After incubation for 4 h, cells were washed twice with PBS and harvested. Detergent extracts were prepared, and Insig-1 was precipitated with anti-Myc.
View Metrics. Calculate the greatest highest common factor divisor , gcf gcd. Sun L. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide. National Center for Biotechnology Information , U.
Fraction 8/ to Decimal Number Equivalent
Sign In Forgot password? To reduce a fraction, divide both its numerator and denominator by their greatest common factor, GCF. Pentchev P. Wei J. Power Solutions for Durable Communication Systems. Support Center Support Center. Open in a separate window. The other proteins include 3-hydroxymethylglutaryl-CoA reductase an ER-bound enzyme whose degradation is accelerated by sterols 28 , 29 ; NPC1, a protein involved in the transport of cholesterol from lysosomes to the ER and to the plasma membrane 30 ; and Patched, which is the receptor for Hedgehog, the only protein known to contain covalently bound cholesterol No detectable amounts of Loop 1 were secreted into the medium.
The endoplasmic reticulum ER 4 protein Scap is unique in nature because it serves as a cholesterol sensor that ensures the proper amount of cholesterol in membranes of animal cells 1 , 2. In contrast, the vast majority of Scap YA was found in a lacy pattern corresponding to ER, and there was no specific localization to the Golgi Fig. No blank values were subtracted. Buffer A contained 50 m m Tris-chloride pH 7.
However, recent biochemical and crystallographic studies showed that the initial sterol-binding site in NPC1 is not contained in the transmembrane segment but rather lies in the N-terminal domain of the protein, which, like Loop 1 of Scap, projects into the lumen of the lysosome 33 , Our previous cholesterol-binding studies were performed with a recombinant form of Scap that contained the entire membrane attachment domain TM1—8 1 ,