From Wikipedia, the free encyclopedia
Pepsin B
Identifiers
EC no. 3.4.23.2
CAS no. 9025-48-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Pepsin B ( EC 3.4.23.2, parapepsin I, pig gelatinase) is an enzyme. [1] This enzyme catalyses the following chemical reaction

Degradation of gelatin, with manor activity on hemoglobin. Specificity for B chain of insulin is more restricted than that of pepsin A

This enzyme is formed from pig pepsinogen B.

See also

References

  1. ^ Ryle AP (1970). Perlmann GE, Lorand, L (eds.). The porcine pepsins and pepsinogens. Methods in Enzymology. Vol. 19. pp. 316–336. doi: 10.1016/0076-6879(70)19023-9.
From Wikipedia, the free encyclopedia
Pepsin B
Identifiers
EC no. 3.4.23.2
CAS no. 9025-48-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Pepsin B ( EC 3.4.23.2, parapepsin I, pig gelatinase) is an enzyme. [1] This enzyme catalyses the following chemical reaction

Degradation of gelatin, with manor activity on hemoglobin. Specificity for B chain of insulin is more restricted than that of pepsin A

This enzyme is formed from pig pepsinogen B.

See also

References

  1. ^ Ryle AP (1970). Perlmann GE, Lorand, L (eds.). The porcine pepsins and pepsinogens. Methods in Enzymology. Vol. 19. pp. 316–336. doi: 10.1016/0076-6879(70)19023-9.

Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook