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Food and feed safety of a novel Vip3C insecticidal protein derived from Paenibacillus spp. for protection of crop plants against key Lepidopteran pests. [PDF]

open access: yesPLoS One
McKinnon LJ   +11 more
europepmc   +1 more source
Some of the next articles are maybe not open access.

Nomenclature of the Pepsins

Nature, 1967
THE Commission on Enzymes of the International Union of Biochemistry1 recommends that the highly active pepsin prepared from pig gastric mucosa2 which is presumed quantitatively to be the principal pepsin should retain the name originally given to it, pepsin A; the other pig pepsins3,4, initially called parapepsins, should be named B.
D J, Etherington, W H, Taylor
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The adsorption of pepsin

The American Journal of Digestive Diseases, 1961
1. The most powerful adsorbents of pepsin are aluminum hydroxide gel and charcoal. 2. The adsorbent action of pepsin is uninfluenced by the substrate concentration and is less active at lowpH levels. When used to inactivate pepsin, the adsorbent effect of aluminum hydroxide gel is more important than thepH effect. 3.
D W, PIPER, B, FENTON
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Coloured inhibitors of pepsin

Biochimica et Biophysica Acta (BBA) - Enzymology, 1967
It was shown that d iazoace ty l -D,L-nor leuc ine inactivates hog pepsin in the presence of copper ions at pH 5; moreover , one residue of the inhibitor is added to the enzyme molecule [1]. It is believed that the inhibitor es ter i f ies one of the carboxyl groups of the enzyme.
V M, Stepanov   +2 more
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AN INSOLUBILISED PEPSIN

International Journal of Peptide and Protein Research, 1972
A highly active insoluble form of pepsin has been prepared for use in isolation of pepsin C inhibitor, a purpose for which it eventually proved ineffective. The preparation may be of interest to others.
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Pepsin as an Esterase

Journal of the American Chemical Society, 1967
K, Inouye, J S, Fruton
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Pepsin

Medical Clinics of North America, 1974
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