Biochem/physiol Actions

Preferentially cleaves C-terminal to Phe, Leu and Glu. It does not cleave at Val, Ala or Gly. pH optimum 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH > 6.

General description

Pepsin is an enzyme found in gastric secretion.

包装

10000, 25000, 50000 units in poly bottle

Quantity

One gram solid swells to 5-10ml packed gel.

Unit Definition

One unit will produce a ΔA₂₈₀ of 0.001 per min at pH 2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 mL. Light path = 1 cm.)

Physical form

Lyophilized powder stabilized with lactose; contains 20% agarose

Application

Pepsin immobilized onto agarose beads can be used to digest and then separate out the active peptides of the glycoprotein gliadin.

Pepsin-agarose has been used as an immobilization tool to investigate the refolding ability of the pepsin enzyme. It has also been used for the preparation of F(ab′)2 fragments from rabbit IgG.

Used to produce F(ab′)₂ fragments of antibodies.¹