Proteins and Derivatives
Proline Specific Endopeptidase (From Flavobacterium Meningosepticum), 50 U
Proline Specific Endopeptidase specifically cleaves peptide bonds on the carboxy side of proline residues. Much slower hydrolysis is observed on the carboxy side of alanine residues. This enzyme is very close, in its properties, to a post-proline cleaving enzyme. The substrates have been found to have the general structure Y-Pro-X, where Y is a peptide or N-protected amino acid and X may be an amino acid, peptide, amide or ester.
Albumin, Human, fraction V (fatty acid free), 5 g
Tested negative for the presence of Hepatitis B Surface Antigen (HBsAg), HIV I/II, HIV-1Ag, HCV, ALT and Syphilis