Pepsin inhibitor from roots of Anchusa strigosa

1998 ◽  
Vol 48 (2) ◽  
pp. 217-221 ◽  
Author(s):  
Ghaleb M. Abuereish
Keyword(s):  
Pepsin Inhibitor

Expression, Purification, and Characterization of the Recombinant Pepsin Inhibitor from Ascaris suum

1998 ◽  
pp. 387-389 ◽  
Author(s):  
Jeffrey Zalatoris ◽  
Chetana Rao-Naik ◽  
Gregory Fecho ◽  
Karen Girdwood ◽  
John Kay ◽  
...  
Keyword(s):  
Ascaris Suum ◽  
Purification And Characterization ◽  
Pepsin Inhibitor

scholarly journals Structure Elucidation of New Pepsin Inhibitor (S-PI)

1971 ◽  
Vol 35 (8) ◽  
pp. 1310-1312 ◽  
Author(s):  
Masayuki FUKUMURA ◽  
Shuzo SATOI ◽  
Noriaki KUWANA ◽  
Sawao MURAO
Keyword(s):  
Structure Elucidation ◽  
Pepsin Inhibitor

scholarly journals ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF PEPSIN INHIBITOR

1941 ◽  
Vol 24 (3) ◽  
pp. 325-338 ◽  
Author(s):  
Roger M. Herriott
Keyword(s):  
Molecular Weight ◽  
Isoelectric Point ◽  
Specific Activity ◽  
Milk Clotting ◽  
Pepsin Inhibitor

A method has been described for the isolation and crystallization of swine pepsin inhibitor from swine pepsinogen. Solubility experiments and fractional recrystallization show no drift in specific activity. The reversible combination of pepsin with the inhibitor was found to obey the mass law. The inhibitor is quite specific, failing to act on other proteolytic and milk clotting enzymes. The inhibitor is destroyed by pepsin at pH 3.5. Chemical and physical studies indicate that the inhibitor is a polypeptide of approximately 5,000 molecular weight with an isoelectric point at pH 3.7. It contains arginine, tyrosine, but no tryptophane and has basic groups in its structure.

The Inactivation of Penicillopepsin with l,2-Epoxy-3-(p-nitrophenoxy)propane, an Active-Site Directed Reagent

1974 ◽  
Vol 52 (11) ◽  
pp. 1018-1023 ◽  
Author(s):  
G. Mains ◽  
T. Hofmann
Keyword(s):  
Methyl Ester ◽  
Aspartic Acid ◽  
Active Site ◽  
Side Chain ◽  
Porcine Pepsin ◽  
Protein Inactivation ◽  
Pepsin Inhibitor

Penicillopepsin was fully inactivated by the pepsin inhibitor 1,2-epoxy-3-(p-nitrophenoxy) propane, and 1.3 ± 0.3 mol of reagent became associated with each mole of protein. Inactivation was more rapid at pH 3.0 than at pH 6.0. Approximately 1 equivalent of the bound reagent was esterified to an aspartic acid side chain. Enzyme previously inactivated with diazoacetylnorleucine methyl ester did not react with the epoxide; and enzyme that was first inactivated with the epoxide did not react with the diazo inhibitor. The results add further evidence for the enzymatic similarity of porcine pepsin and penicillopepsin.

Studies on the interaction between Streptomyces pepsin inhibitor and several acid proteinases by means of a zinc(II)-dye complex as a probe

1975 ◽  
Vol 391 (2) ◽  
pp. 415-421 ◽  
Author(s):  
Hiroshi Nakatani ◽  
Keitaro Hiromi ◽  
Shuzo Satoi ◽  
Kohei Oda ◽  
Sawao Murao ◽  
...  
Keyword(s):  
Pepsin Inhibitor

Improved pepsin inhibitor derived from activation peptide 1-16 of porcine pepsinogen

Biochemistry ◽  
1977 ◽  
Vol 16 (17) ◽  
pp. 3846-3849 ◽  
Author(s):  
P. M. Harish Kumar ◽  
Beatrice Kassell
Keyword(s):  
Activation Peptide ◽  
Pepsin Inhibitor

scholarly journals Effect of Pepsin Inhibitor (S-PI) on the Growth of Rhodotorula glutinis No. K-24

1972 ◽  
Vol 36 (11) ◽  
pp. 2041-2043 ◽  
Author(s):  
Sawao MURAO ◽  
Motoo ARAI ◽  
Kunio NAKAHARA ◽  
Masami TSUCHIYA
Keyword(s):  
Rhodotorula Glutinis ◽  
Pepsin Inhibitor

Binding of Streptomyces pepsin inhibitor (acetyl-pepstatin) with chymosin (rennin)

1980 ◽  
Vol 614 (1) ◽  
pp. 144-150 ◽  
Author(s):  
Hiroshi Nakatani ◽  
Masakazu Tsuchiya ◽  
Tomohiro Morita ◽  
Shigenori Ohki ◽  
Keitaro Hiromi
Keyword(s):  
Pepsin Inhibitor
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