Microchemical analysis section:

Taylor, John Κ.

doi:10.6028/nbs.tn.455

Cited by 2 publications

(3 citation statements)

References 16 publications

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“…The similarity in the C-terminal residues between zymogen and enzyme and the dissimilarity between the N-terminal ones indicates that activation of the zymogen occurs by release of a peptide from the N-terminal end. This is in accord with the activation mechanism of pepsinogens of other species (Taylor, 1968). Further conclusions can be drawn about the activation mechanism from the difference in the rates of reaction of the pepsinogen and pepsin with pchloromercuribenzoate.…”

Section: Properties Ofpepsinogen 4 and The Derivedpepsinsupporting

confidence: 89%

“…Comparison ofpepsinogens and pepsins from chicken with those from other species All species on which detailed investigations have been made secrete more than one gastric proteinase. This applies to the human, pig (Taylor, 1968), dogfish (Merrett et al, 1969) and ox (Lang & Kassell, 1971;Antonini & Ribadeau-Dumas, 1971), and the chicken is no exception.…”

Section: Properties Ofpepsinogen 4 and The Derivedpepsinmentioning

confidence: 99%

“…The stomachs of all vertebrates investigated secrete a number of enzymes with proteinase activity at acid pH values (Taylor, 1968). The two stomach proteinases that have been studied in greatest detail are pig pepsin A (EC 3.4.4.1) and calfrennin (EC 3.4.4.3).…”

mentioning

confidence: 99%

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The purification and properties of a single chicken pepsinogen fraction and the pepsin derived from it

Green¹,

Llewellin²

1973

Biochemical Journal

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1. Evidence is given for the presence of at least five pepsinogens in a crude extract of mixed chicken stomachs. One of these was purified and could be activated to yield a single pepsin. 2. The molecular weights of the pepsinogen and pepsin were 36000 and 34000 respectively. The pepsin associated at low pH values and low ionic strength. 3. The amino acid analyses of both proteins are given. The pepsin was devoid of phosphate but contained carbohydrate. 4. The N-terminal amino acids of pepsinogen and pepsin were serine and threonine respectively. Five amino acids were released by carboxypeptidase A and it was deduced that serine may be the C-terminal one. 5. Each protein contained one thiol group per molecule as determined by titration with p-chloromercuribenzoate. The rate of the reaction was very rapid with pepsin, but much slower with pepsinogen, although the same group appeared to react in both instances. The enzymic activity of pepsin was unaffected by the modification. 6. The isoionic point of the pepsin was close to pH4.0 and the enzyme was stable for long periods at pH values up to 7.0. 7. The enzyme hydrolysed bisphenyl sulphite almost as rapidly as did pig pepsin A.

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Section: Properties Ofpepsinogen 4 and The Derivedpepsinsupporting

confidence: 89%