Enzyme envelopes on colloidal particles

Haynes, Royce; Walsh, Kenneth A.

doi:10.1016/0006-291x(69)90320-9

Cited by 89 publications

(12 citation statements)

References 15 publications

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“…4-6 suggests that only a limited number of binding sites were available for the inhibitors (since both inhibitors have pl's below 5.0, they were negatively charged under the reaction conditions, and the obtained results could not be explained by any electrostatic repulsion effect between inhibitor and carrier). Previous findings with silica-adsorbed/glutaraldehyde-cross linked trypsin indicated that the effectiveness of natural trypsin inhibitors with the immobilized enzymes was inversely related to their sizes (Haynes and Walsh, 1969). A similar conclusion may be drawn from the presents results.…”

Section: Resultssupporting

confidence: 88%

Immobilization of proteinases on Chitosan

Leuba

Widmer

1979

Biotechnol Lett

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SUMMARYTrypsin, pronase and subtilisin were immobilized on chitosan by glutaraldehyde coupling. Significant retention of activity was observed when synthetic substrates as well as casein were used. The specific activities of the bound proteinases ranged from 38% to 79% of their initial specific activities. The pH-activity profile of trypsin was slightly shifted toward alkaline values, and its thermal stability was increased. Immobilized trypsin was found to be less sensitive to its natural inhibitors than the soluble enzyme.

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Section: Resultssupporting

confidence: 88%

Immobilization of proteinases on Chitosan

Leuba

Widmer

1979

Biotechnol Lett

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“…Free ε-amino groups that react with FDNB also may react with glutaraldehyde and produce supernumerary cross-links. Cross-linking with glutaraldehyde forms intermolecular bonds highly resistant to degradation by proteolytic enzymes [ 41 ]. In concentrations below 5 mM/liter, glutaraldehyde reduces the yield of bone little or not at all, whereas in concentrations of 5 to 10 mM/liter, the reduction is from 10 to 40%.…”

Section: Discussionmentioning

confidence: 99%

The Classic: Bone Morphogenetic Protein

Urist¹,

Strates²

2009

Clin Orthop Relat Res

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This Classic Article is a reprint of the original work by Marshall R. Urist and Basil S. Strates, Bone Morphogenetic Protein. An accompanying biographical sketch of Marshall R. Urist, MD is available at DOI 10.1007/s11999-009-1067-4; a second Classic Article is available at DOI 10.1007/s11999-009-1069-2; and a third Classic Article is available at DOI 10.1007/s11999-009-1070-9. The Classic Article is © 1971 by Sage Publications Inc. Journals and is reprinted with permission from Urist MR, Strates BS. Bone morphogenetic protein. J Dent Res . 1971;50:1392–1406.

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“…Extremely reduced coagulant activity was apparently related to steric limita tions on the penetration of the high molecular weight fibrinogen substrate. Several immobilized derivatives of proteolytic enzy mes, including bovine thrombin, have been reported to hydrolize proteins only at a fraction of the rate expected on the basis of their catalytic activities determined when low molecular weight sub strates were used (20). Similar limitations may be imposed in case of enzyme inhibition.…”

Section: Discussionmentioning

confidence: 99%

The Interaction of Immobilized Thrombin with Human Antithrombin III

Marciniak

Gora-Maslak

1984

Thromb Haemost

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SummaryInteraction of human antithrombin III (AT III) with human α-thrombin coupled to Sepharose 4B was investigated. Despite markedly reduced esterolytic, amidolytic and especially coagulant activity, more than 90% of immobilized thrombin formed stable complexes with purified AT III. Presence of high affinity heparin did not facilitate the inhibition to the degree seen in reactions conducted with soluble thrombin. Instead, heparin induced proteolysis of up to 66% of the inhibitor that remained in solution. This led to the isolation of a homogeneous protein fragment which migrated in SDS-gel electrophoresis as a band of 50,000 Mr, cross-reacted with antibodies to human AT III but showed no biologic activity nor sufficient affinity for heparin. Out of the three major inhibitors capable of binding soluble thrombin in human plasma, only AT III reacted with immobilized thrombin. However, Sepharose-coupled thrombin mixed with plasma in the presence of heparin produced outstanding quantities of residual immunoreactive AT III devoid of inhibitory activity. These data suggest that presence of high affinity heparin in the environment of thrombin attached to a solid support may dramatically decrease the efficiency of enzyme inhibition.

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Enzyme envelopes on colloidal particles

Cited by 89 publications

References 15 publications

Immobilization of proteinases on Chitosan

Immobilization of proteinases on Chitosan

The Classic: Bone Morphogenetic Protein

The Interaction of Immobilized Thrombin with Human Antithrombin III

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