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Thermo Scientific Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic, or hydrophobic amino acids. The Proteinase K is classified as a serine protease (see Reference 1). The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.
W. Ebeling et al., Proteinase K from Tritirachium album Limber. Eur. J. Biochem. 47, 91-97 (1974).
U. Wiegers, H. Hilz, A new method using ‘proteinase K’ to prevent mRNA degradation during isolation from HeLa cells. Biochem. and Biophys. Res. Commun. 44(2), 513-519 (16 July 1971).
H. Hilz et al., Stimulation of proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of “masked” proteins. Eur. J. Biochem. 56(1), 103-108 (1 August 1975).
D. Brdiczka, W. Krebs, Localization of enzymes by means of proteases. Biochim. Biophys. Acta. 297(2), 203-212 (1973).
J. S. Crowe et al., Improved cloning efficiency of polymerase chain reaction (PCR) products after proteinase K digestion. Nucleic Acids Res. 19, 184 (1991).
K. D. Jany et al., Amino acid sequence of Proteinase K from mold Tritirachtum album Limber Proteinase K – a subtilisn related enzyme with disulfide bonds. FEBS Lett. 199, 139-144 (1986).
J. Bajorath et al., The enzymatic activity of proteinase K is controled by calcium. Eur. J. Biochem. 176, 441-447 (1988).
W. Ardelt, M. Laskowski Jr., Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same ...Leu18-Glu19... reactive site. Biochemistry. 24(20), 5313-5320 (24 September 1985).