Biology
- Q: Explain The Effects Of Too High A Temperature On An Enzyme
If the temperature is too high, an increase in kinetic energy of the molecules will cause excessive vibrations of the molecules. This will disrupt the 3 dimensional structure of the enzyme, causing it to become a random coil. The enzyme is therefore denatured....
- Q: Distinguish Between Competitive And Non-competitive Inhibition Of Enzymes
A competitive inhibitor is structurally similar to the substrate but a non-competitive inhibitor is often structurally different from the substrate. Hence, a competitive inhibitor will compete with the substrate for an active site but a non competitive...
- Tryptophan (trp W)
Term: tryptophan (Trp W)Literally meaning: ?to be broken and to appear?Origin: Anc Greek?????/trivo (=to rub, to powder, to grind) > (simple past) ??????/etrips? >????/tryo(=to puncture)?????/pheno(=be visible, or obvious, show)Coined/History ...
- Elastase
Term: elastaseLiterally meaning: ?separating elastin?Origin: Anc Greek ????/elao(=be flexibe or ductile)) >??????/elavno(=run, drive)-???/-asy(=-ase) suffix added to the name of the substrate that the enzyme hydrolyzes eg proteinase for protein...
- Pepsin
Term: pepsinLiterally meaning: ?protein of digesting?Origin: Anc Greek?????/pepto(=digest)Coined/HistoryThe term coined by German physiologist Theodor Schwann in the early 19th century when he identified a chemical agent in the stomachs of animals...
Biology
chymotrypsin
Term: chymotrypsin
Literally meaning: ?protein of rubbing juices?
Origin: Greek
?????/chymos(=juice) > ???/cheo(=pour)
+ ?????/trivo (=rub, powder, grind) > (simple past) ?????? /etrips?
Coined/History
In 1934 M. ?unitz and J.H.Northrop were able to isolate and crystallize from pancreatic preparations an enzyme, in adition to trypsin, named chemotrypsin as well as the inactive precursor, chymotrypsinogen (J. Gen. Physiol., 17, 1934). Four years later Kunitz was able to isolate different active forms of the enzyme called them as alpha, beta, and gama.
Definition
Chymothrepsin is a proteolytic enzyme that cleaves the peptide bonds at carboxy site of aromatic residues (tyrosine, phenylalanine, and tryptophan). Chymotrepsin is active in the intestine produced by the acinar cells of the pancreas. Chymotrepsin becomes activated after proteolysis of chemotrypsinogen by trypsin.
- Q: Explain The Effects Of Too High A Temperature On An Enzyme
If the temperature is too high, an increase in kinetic energy of the molecules will cause excessive vibrations of the molecules. This will disrupt the 3 dimensional structure of the enzyme, causing it to become a random coil. The enzyme is therefore denatured....
- Q: Distinguish Between Competitive And Non-competitive Inhibition Of Enzymes
A competitive inhibitor is structurally similar to the substrate but a non-competitive inhibitor is often structurally different from the substrate. Hence, a competitive inhibitor will compete with the substrate for an active site but a non competitive...
- Tryptophan (trp W)
Term: tryptophan (Trp W)Literally meaning: ?to be broken and to appear?Origin: Anc Greek?????/trivo (=to rub, to powder, to grind) > (simple past) ??????/etrips? >????/tryo(=to puncture)?????/pheno(=be visible, or obvious, show)Coined/History ...
- Elastase
Term: elastaseLiterally meaning: ?separating elastin?Origin: Anc Greek ????/elao(=be flexibe or ductile)) >??????/elavno(=run, drive)-???/-asy(=-ase) suffix added to the name of the substrate that the enzyme hydrolyzes eg proteinase for protein...
- Pepsin
Term: pepsinLiterally meaning: ?protein of digesting?Origin: Anc Greek?????/pepto(=digest)Coined/HistoryThe term coined by German physiologist Theodor Schwann in the early 19th century when he identified a chemical agent in the stomachs of animals...