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).<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).<br /> | ||
*'''Endothiapepsin''' is an '''aspartic PRO''' from ''Cryphonectria parasitica''.<br /> | *'''Endothiapepsin''' is an '''aspartic PRO''' from ''Cryphonectria parasitica''<ref>PMID:1525155</ref>.<br /> | ||
*'''Saccharopepsin''' is an '''aspartic PRO''' from yeast.<br /> | *'''Saccharopepsin''' is an '''aspartic PRO''' from yeast<ref>PMID:17447722</ref>.<br /> | ||
*'''Falcipain''' is an '''cystein PRO''' from ''Plasmodium falciparum''.<br /> | *'''Falcipain''' is an '''cystein PRO''' from ''Plasmodium falciparum''<ref>PMID:21660657</ref>.<br /> | ||
For '''cysteine PRO''' from ''Trypanosoma cruzi'' see [[Cruzain]]. | For '''cysteine PRO''' from ''Trypanosoma cruzi'' see [[Cruzain]]. | ||