Binding of bovine plasminogen to immobilized casein and its activation thereon

Baer, A.; Ryba, I.; Collin, J.C.

doi:10.1016/0958-6946(94)90036-1

Cited by 16 publications

(10 citation statements)

References 24 publications

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“…The activity of PL or PAs may be inhibited by plasmin inhibitors (PIs) or plasminogen activator inhibitors (PAIs), respectively (Precetti, Oria, & Nielsen, 1997). Unlike PL, PG, and PAs, which associate with casein micelles (Baer, Ryba, & Collin, 1994;Grufferty & Fox, 1988;Haissat et al, 1994;Politis, Barbano, & Gorewit, 1992;White et al, 1995), the inhibitors are found in the serum fraction of fluid milk (Reimerdes, Klostermeyer, & Sayk, 1976).…”

Section: Introductionmentioning

confidence: 97%

Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk

Prado

Sombers

Ismail

et al. 2006

International Dairy Journal

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Section: Introductionmentioning

confidence: 97%

Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk

Prado

Sombers

Ismail

et al. 2006

International Dairy Journal

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“…Plasminogen activators (PAs) are serine proteinases responsible for the conversion of plasminogen to plasmin (Lu & Nielsen, 1993;Heegaard, Rasmussen, & Andreasen, 1994;White et al, 1995). The caseins act as an immobilisation matrix for plasminogen activation (Baer, Ryba, & Collin, 1994;Politis, White, Zativon, Goldberg, Gou, & Kinstedt, 1995). The close proximity of plasmin to its substrate ensures that hydrolysis is an efficient process (Korycka-Dahl, Ridadeau Dumas, Chene, & Martal, 1983).…”

Section: Introductionmentioning

confidence: 98%

Factors affecting the hydrolytic action of plasmin in milk

Crudden

Patrick

Fox

et al. 2005

International Dairy Journal

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“…Several ELISA methods have been developed to measure PL and PG concentrations in milk and cheese samples (Politis et al, 1992;Baer et al, 1994;Benfeldt et al, 1995;. However, application of ELISA is limited by the lack of availability of high quality monoclonal antibodies that differentiate PL from PG.…”

Section: Introductionmentioning

confidence: 99%

Fluorescent Labeling Study of Plasminogen Concentration and Location in Simulated Bovine Milk Systems

Wang

Hayes

Mauer

2006

Journal of Dairy Science

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A fluorescent labeling method was developed to study plasminogen (PG) concentration and location in simulated bovine milk. Activity and stability of PG labeled with Alexa Fluor 594 (PG-594) were comparable to those of native PG. The fluorescent signal of PG-594 exhibited pH, temperature, and storage stability, and remained stable throughout typical sample treatments (stirring, heating, and ultracentrifugation). These characteristics indicate broad applicability of the fluorescent labeling technique for milk protease characterization. In an example application, PG-594 was added to simulated milk samples to study effects of heat and beta-lactoglobulin (beta-LG) on the distribution of PG. Before heating, about one-third of the PG-594 remained soluble in the whey fraction (supernatant) whereas the rest became associated with the casein micelle. Addition of beta-LG to the system slightly shifted PG-594 distribution toward the whey fraction. Heat-induced PG-594 binding to micelles in whey-protein-free systems was evidenced by a decrease of PG-594 from 31 to 15% in the whey fraction accompanied by an increase of PG-594 from 69 to 85% in casein micelle fractions. When beta-LG was present during heating, more than 95% of PG-594 became associated with the micelle. A comparison with the distribution pattern of PG-derived activities revealed that heat-induced PG binding to micelles accompanies heat-induced PG inactivation in the micelle fraction. Incubation of the casein micelles with the reducing agent beta-mercaptoethanol revealed that disulfide bonds formed between PG and casein or between PG and casein-bound beta-LG are the mechanisms for heat-induced PG binding to casein micelles. Western blotting and zymography results correlated well with fluorescent labeling studies and activity studies, respectively. Theoretically important findings are: 1) when heated, serum PG is capable of covalently binding to micellar casein or complexing with beta-LG in whey and then coadhering to micelles, and 2) PG that associated with micellar casein through lysine binding sites before heating is capable of developing heat-induced disulfide bonds with casein. The overall results are PG covalently binding to micelles and inactivation thereafter. Our results suggest that, instead of thermal denaturation through irreversible unfolding, covalent bond formation between PG and other milk proteins is the mechanism of PG inhibition during thermal processing.

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Binding of bovine plasminogen to immobilized casein and its activation thereon

Cited by 16 publications

References 24 publications

Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk

Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk

Factors affecting the hydrolytic action of plasmin in milk

Fluorescent Labeling Study of Plasminogen Concentration and Location in Simulated Bovine Milk Systems

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