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P3270-01 Anti-Pepsin, 10,000+ U/mg (Porcine), NF/USP

Specifications
References
Grade
Reagent Grade
Shipping Temp
RT
Storage Temp
-20°C
EC=3.4.23.1; Porcine stomach

Pepsin, an acidic protease, is the principal proteolytic enzyme of vertebrate gastric juice. Its inactive precursor, pepsinogen, is produced in stomach mucosa. Pepsin has a broad range of substrates and demonstrates an esterase activity. There are several minor pepsins designated “B”, “C”, and “D”; the major component is “A” to which the following data applies. They are chromatographically separable.

Conversion of pepsinogen to pepsin, which involves releasing a peptide, may be an autocatalytic process involving self-cleavage by the zymogen. Peptides released on activation have pepsin inhibitory activity.
CAS No
9001-75-6
Molecular Weight
~35kD
Source
Porcine stomach
Appearance
White to slight yellow, powder
Identification
Conforms
Loss on Drying
≤5%
Protease Activity
≥10,000U/mg [The activity of pepsin (10,000U/mg) is the same as strength (1:10,000NF).]
Solubility
Soluble in Water. Mostly insoluble in alcohol
Total Bacteria
≤10,000cfu/g
Yeast and Mold
≤100cfu/g
Bile-Tolerant Gram-Negative Bacteria
≤100cfu/g
E. coli
Negative/g
S. aurues
Negative/g
Salmonella
Negative/g
Optimum pH
~1.0 for such substrates as casein or hemoglobin if the substrate is native.
Inhibitors
Substrate-like epoxides
Storage and Stability
Powder may be stored at -20°C Stable for 6 months after receipt.
Note
Meets or exceeds USP/NF Specifications
Form
White to slight yellow, powder.
References
1. Al-Janabi, et al., J. Biol. Chem., 247:4628 (1972). 2. Anderson, W., et al., Nature, 243:417 (1973). 3. Andreeva, N.: Scand. J. Clin. Lab Invest., 52, Suppl. 210:31 (1992) 4. Anson, M.: J. Gen. Physiol., 22:79 (1938). 5. Arnon, R., and Perlmann, G.: J. Biol. Chem., 238:653 (1963) 6. Auer, H., and Glick, D.: Biochem., 23:2735 (1984) 7. Baker, L.: J. Biol. Chem., 211:701 (1954) 8. Basson, M., et al., J. Surgical Res., 44:82 (1988) 9. Bayliss, R., Knowles, J., and Wybrandt, G.: Biochem. J., 113:377 (1969) 10. Blumenfeld, O., and Perlmann, G.: J. Gen. Physiol., 42:563 (1959) 11. Blumenfeld, O., and Perlmann, G.: J. Gen. Physiol., 42:553 (1959). 12. Blumenfeld, et al., J. Biol. Chem., 235:379 (1960). 13. Bovey, F., and Yanari, S.: Pepsin, in The Enzymes, Vol. IV, (Boyer, P., Lardy, H., and Myrback, K., eds.), Academic Press, NY, 63 (1960). 14. Bustin, M., and Conway-Jacobs, A.: Intramolecular Activation of Porcine Pepsinogen, J. Biol. Chem., 246:615 (1971). 15. Chen, K., and Tang, J.: Amino Acid Sequence Around the Epoxide-Reactive Residues in Pepsin, J. Biol. Chem., 247, 2566 (1972). 16. Chen, K., et al., J. Biol. Chem., 250:5068 (1975).
USBio References
No references available
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