Chemical modification and cross-linking of proteins by impurities in glycerol

Bello, Jake; Bello, Helene R.

doi:10.1016/0003-9861(76)90114-4

Cited by 38 publications

(11 citation statements)

References 4 publications

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“…A recent study on the impurities in commercial glycerol (25) raised the possibility that the observed inhibition of platelet aggregation was the result of the cross-linking of proteins by these impurities. However, the results presented in Fig.…”

Section: Discussionmentioning

confidence: 99%

Borate and glycerol inhibition of the aggregation of guinea pig platelets by bovine factor VIII and ristocetin

Kuwahara

1977

American J Hematol

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To demonstrate the importance of the carbohydrate portions of bovine factor VIII and ristocetin for the induction of platelet aggregation, guinea pig platelets were treated with either borate or glycerol before and after addition of ristocetin or bovine factor VIII. Both borate and glycerol were capable of inhibiting the aggregation of blood platelets induced by adding bovine factor VIII or ristocetin to platelet-rich plasma. Furthermore, aggregates formed after treatment with either agent could be dispersed by high concentrations of either borate or glycerol. These effects did not appear to be solely the result of high ionic strength or of irreversible damage to the platelets. The results obtained support the hypothesis that the binding of the carbohydrate groups of factor VIII plays an important role in the induction of platelet aggregation and in the maintenance of aggregates formed in response to the treatment of platelet-rich plasma with bovine factor VIII or ristocetin.

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Section: Discussionmentioning

confidence: 99%

Borate and glycerol inhibition of the aggregation of guinea pig platelets by bovine factor VIII and ristocetin

Kuwahara

1977

American J Hematol

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“…Such reaction products are able to undergo Amadori rearrangement (Acharya and Manning, 1983) which generates new carbonyl functions capable offorming Schiff base linkages with other amino groups . Eventually such reactions result in covalent cross-linking of the protein (Acharya and Manning, 1983;Bello and Bello, 1976). Thus, in addition to insulin 's potential to form CID by transamidation reactions (Helbig, 1976;Brange 1992), the CID can also be generated via an initial reaction with aldehydes.…”

Section: Kinetics and Mechanismsmentioning

confidence: 99%