Cross linking of proteins <i>in vitro</i> by peroxidase

Stahmann, Mark A.; Spencer, A. K.; Honold, Guy R.

doi:10.1002/bip.1977.360160611

Cited by 57 publications

(21 citation statements)

References 23 publications

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“…In this situation, close apposition of the molecules is a precondition for successful cross-linking (39). In addition, cross-linking of lysine-containing proteins by a similar oxidative mechanism has been achieved with hydrogen peroxide, myeloperoxidase, and catechol (17,40,41). In this case, the resulting quinone mediates the oxidative deamination of lysine with the formation of aldehydes that react with other aldehydes by aldol condensation, and with amino groups to form Schiff bases (41).…”

Section: Discussionmentioning

confidence: 99%

Oxidative cross-linking of immune complexes by human polymorphonuclear leukocytes.

Jasin

1988

J. Clin. Invest.

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Incubation of human serum albumin-anti-human serum albumin immune complexes bound to a plastic surface, with human polymorphonuclear leukocytes for I h at 370C resulted in covalent cross-linking of 8.5%±0.5 of the complexes, corresponding to a minimum rate of 700 antibody molecules per cell per minute. Similar results were obtained with IgG-anti-IgG and type II collagen-anticollagen II human antibodies. Crosslinking was defined as the antibody remaining attached to plastic-bound antigen after extraction with 3 M MgCl2 and 0.1 N HCl solutions. The effects of addition of oxygen radical scavengers, heme-enzyme inhibitors, and omission of Cl-indicated that the cross-linking process was mediated by the myeloperoxidase-H202-Cl system. Cross-linking was also obtained with cell lysates, polynorphonuclear granules, and purified human myeloperoxidase in the presence of a steady flux of H202 provided by glucose oxidase-glucose. Cross-linking by the cell-free systems was also abolished by sodium azide or omission of chloride ions.Cross-linked immune complexes were also generated by incubation with 20 to 50 ,uM solutions of freshly distilled hypochlorous acid. Addition of 10 mM hypochlorous acid to soluble IgG resulted in the formation of protein precipitates insoluble in 5 M guanidine, 0.1 N HC1, or boiling 2.3 M sodium dodecyl sulfate-1.4 M 2-mercaptoethanol. The remaining soluble IgG contained fluorescent high molecular aggregates (ex: 360 nm; em: 454 nm). Oxidative cross-linking of antigen-antibody molecules, and of immune complexes to connective tissue macromolecules may play a pathogenic role in acute and chronic inflammatory processes.

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Section: Discussionmentioning

confidence: 99%

Oxidative cross-linking of immune complexes by human polymorphonuclear leukocytes.

Jasin

1988

J. Clin. Invest.

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“…The peroxidase-catalyzed cross-linking of ␣-lactalbumin can most simply be described by the following reaction sequences: 2N␣-lac → N(␣-lac) 2 (1)…”

Section: Correlation Between Reacted˛-lactalbumin and Increase In Absmentioning

confidence: 99%

“…A quite novel approach in food protein crosslinking is enzymatic oxidation. The use of laccase and peroxidase to cross-link proteins has been well described [1][2][3]. By catalyzing the conversion of tyrosine residues to phenolic radicals, peroxidase (EC 1.11.1.7) can initiate the formation of dityrosines [4] and trityrosines (in vivo) [5].…”

Section: Introductionmentioning

confidence: 99%

In-line quantification of peroxidase-catalyzed cross-linking of α-lactalbumin in a microreactor

Heijnis¹,

Wierenga²,

Janssen³

et al. 2010

Chemical Engineering Journal

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“…Relatively low concentrations of many classes of phenolic compounds have been found to participate in in vitro cross-linking reactions with proteins (Stahmann et al, 1977;Leatham et al, 1980). During studies on the maturation of fruiting bodies of the basidiomycete Polyporus hispidus, it was found that hispidin (a natural phenolic compound) became less susceptible to ethanol extraction as the fruiting body pigmented and became more fibrous and woody (Bu'lock, 1967).…”

Section: G F L E a T H A M A N D M A S T A H M A N Nmentioning

confidence: 99%

Studies on the Laccase of Lentinus edodes: Specificity, Localization and Association with the Development of Fruiting Bodies

1981

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The phenol oxidases from mature fruiting bodies of Lentinus edodes (Berk.) Sing., a commercially cultivated mushroom, were studied. The major phenol oxidase was a laccase with a pH optimum near 4.0 and an apparent molecular weight of 100000. Catechol oxidase and tyrosinase were also present. The laccase investigated was primarily extracellular ; the highest activity was in the pigmented rind of the pileus and in the stipe. Increased laccase activity was associated with rapid growth of non-pigmented aerial mycelium and formation of pigmented primordia and fruiting bodies. Possible functions of the laccase and its regulation during the development of fruiting bodies are discussed.

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Cross linking of proteins in vitro by peroxidase

Cited by 57 publications

References 23 publications

Oxidative cross-linking of immune complexes by human polymorphonuclear leukocytes.

Oxidative cross-linking of immune complexes by human polymorphonuclear leukocytes.

In-line quantification of peroxidase-catalyzed cross-linking of α-lactalbumin in a microreactor

Studies on the Laccase of Lentinus edodes: Specificity, Localization and Association with the Development of Fruiting Bodies

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