1974
DOI: 10.3891/acta.chem.scand.28b-1098
|View full text |Cite
|
Sign up to set email alerts
|

The Use of Ethylene Maleic Anhydride for the Preparation of a Water-soluble Polyanionic Derivative of Pepsin. Preparation and Properties.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
8
0

Year Published

1975
1975
1991
1991

Publication Types

Select...
4
3

Relationship

0
7

Authors

Journals

citations
Cited by 11 publications
(8 citation statements)
references
References 0 publications
0
8
0
Order By: Relevance
“…Our results indicate that the stability of pepsin near neutral pH was markedly improved by carboxyl modification. Porcine pepsin is rapidly denatured at pH 7.0 and and Fox, 1974), probably due to an electrostatic expansion of the negatively charged polypeptide chains (Lowenstein, 1974). The decrease in net negative charge on the carboxyl-modified pepsin molecule (Figure 2) may lower the extent of electrostatic expansion and subsequent denaturation.…”
Section: Discussionmentioning
confidence: 99%
See 2 more Smart Citations
“…Our results indicate that the stability of pepsin near neutral pH was markedly improved by carboxyl modification. Porcine pepsin is rapidly denatured at pH 7.0 and and Fox, 1974), probably due to an electrostatic expansion of the negatively charged polypeptide chains (Lowenstein, 1974). The decrease in net negative charge on the carboxyl-modified pepsin molecule (Figure 2) may lower the extent of electrostatic expansion and subsequent denaturation.…”
Section: Discussionmentioning
confidence: 99%
“…The pH stability of both crystalline and crude pepsins was determined by the methods described by Lowenstein (1974) and Green (1972).…”
Section: Determination Of Pepsin Stability Near Neutral Phmentioning
confidence: 99%
See 1 more Smart Citation
“…Lowenstein 16 ) reported a shift of 1.5 pH units toward a more alkaline pH optima following EMA modification of porcine pepsin. A similar trend was obtained in this study; both modified pepsin and chymosin functioned optimally at a pH 0.5 units above native enzyme pH-activity optimum (Fig.…”
Section: C)mentioning
confidence: 99%
“…Increased negative charge through covalent attachment of a polyanionic copolymer to the lysyl residue in porcine pepsin decreased both proteolytic and milk-clotting activities. 16 ) The majority of the studies reporting reduced catalytic activity of chemically modified fungal and mammalian aspartyl proteinases have not found if changes in function were coincident with structural (conformational) changes. In addition, no comparative structure-function study has been done to date on the effects of chemical modification of amino groups in aspartyl proteinases from different (i.e., fungal versus mammalian) sources.…”
mentioning
confidence: 99%