Proteinase: Difference between revisions
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* '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<br /> | * '''PRO A''' is a carboxylproteinase<ref>PMID:6799292</ref>.<br /> | ||
* '''PRO K''' is a serine protease which cleaves proteins preferentially after hydrophobic residues<ref>PMID:9606141</ref>. Calcium ions contribute to the stability of the enzyme. PRO K is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO K is used in the partial proteolysis of lactoferrin into its N- and C-lobe. The two lobes of lactoferrin have different antimicrobial and antifungal properties. PRO K can digest hair (keratin). | * '''PRO K''' is a serine protease which cleaves proteins preferentially after hydrophobic residues<ref>PMID:9606141</ref>. Calcium ions contribute to the stability of the enzyme. PRO K is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO K is used in the partial proteolysis of lactoferrin into its N- and C-lobe. The two lobes of lactoferrin have different antimicrobial and antifungal properties. PRO K can digest hair (keratin). | ||
For cysteine PRO from ''Trypanosoma cruzi'' see [[Cruzain]]. | For '''cysteine PRO''' from ''Trypanosoma cruzi'' see [[Cruzain]]. | ||
=== The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | === The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen-bond density in the reactive loop <ref>doi 10.1080/07391102.2012.745378</ref> === | ||