Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- BIM-46187 is a protein inhibitor that binds to the a-subunit of the G. protein. It prevents the GDP/GTP exchange and prevents activity of the G protein. Which of the following would you expect to see lower levels of as a result? You can select more than or answer. S-S NH2 Mol. M: 795.11 Image: https://aobious.com/aobious/protein-inhibitors/1086-bim-46187.html Select one or more: O a. Cyclic AMP (CAMP) O b. Tyrosine kinase O . HSP O d. Adenylyl Cyclase (AC) O e. DAG O f. JAK O g. IP3arrow_forwardWhat is the importance in glycosylation in rtPA in terms of its activity as a protein therapeutic?arrow_forwardDescribe a common feature at the active site of serine proteases and acetyl cholinesterasearrow_forward
- The objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…arrow_forwardThe following data describe the catalysis of cleavage of peptide bonds in small peptides by a protease: Substrate K (1/s) K₁, (mM) k./K₁ (mM/s) A 0.1 10 B 1 1 10 0.1 100 0.02 8,000 0.05 10,000 0.5 Use this information to answer the next three questions. BODEF с D E F 0.01 1 100 5,000 160,000 20,000 4. Which substrate binds to the enzyme with the highest affinity? a. A b. B C. C d. D e. E f. Farrow_forwardDescribe type I, II, and III L-asparaginases. Mention characteristics and differences between them with respect to enzyme kinetics (rate, km, etc).arrow_forward
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