Solid state lactoperoxidase: A highly stable enzyme for simple, gentle iodination of proteins

David, Gary S.

doi:10.1016/s0006-291x(72)80074-3

Cited by 247 publications

(40 citation statements)

References 20 publications

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“…Neoglycoproteins were labeled with 125I by lactoperoxidase method (24 (26) and Hill (27) (28). Cells were then washed twice with D-PBS in a microcentrifuge and the radioactivities of the supernate and the cell pellet were counted separately as surface bound and internalized, respectively.…”

Section: Methodsmentioning

confidence: 99%

Characterization of membrane homing receptors in two cloned murine hemopoietic progenitor cell lines.

Matsuoka

Hardy²,

Tavassoli³

1989

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

Characterization of membrane homing receptors in two cloned murine hemopoietic progenitor cell lines.

Matsuoka

Hardy²,

Tavassoli³

1989

J. Clin. Invest.

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“…The protein part of apotransferrin was labeled with 125I using lactoperoxidase method (17). When tritiated apotransferrin was labeled, subsequent '25I labeling was done with Bolton-Hunter reagent (18) since the usual peroxidation method could theoretically remove the 3H label from sialic acid.…”

Section: Tf and Labeling Methodsmentioning

confidence: 99%

Desialation of transferrin by rat liver endothelium.

Irie

Kishimoto²,

Tavassoli³

1988

J. Clin. Invest.

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To examine the role of liver endothelium in desialation of transferrin (TF), pulse-chase studies were done by incubation of either 3H (sialic acid labeled)-, or 125I, or 59Fe (protein core labeled)-TF with fractionated liver endothelium. While 1251 or 59Fe labels were externalized after initial binding and internalization, a large proportion of 3H label was internalized and remained within the cell. When the supernatant of these experiments was studied by isoelectricfocusing and Ricinus communis agglutinin (RCA120) affinity chromatography, generation of asialotransferrin was noted by both techniques. Incubation of liver endothelium with double-labeled TF (sialic acids with 3H and protein core with 1251 or 59Fe) led initially to a concordant uptake of the two labels, which were then dissociated and 3H was retained by the cell. These findings indicate desialation of TF by liver endothelium. The significance of these findings in the pathogenesis of hepatic siderosis is discussed.

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“…The ascending limb of the protein peak of the void volume was collected, concentrated by ammonium sulfate precipitation, dialyzed, and used as previously described (7). Labeling of the protein was performed either by use of the technique of limited oxidation of terminal galactose residues by galactose oxidation and reduction of these residues by tritiated [3H]potassium borohydride as previously described (7), or by iodination with 125I by means of immobilized lactoperoxidase (8,9).…”

Section: Methodsmentioning

confidence: 99%

Asialo von Willebrand factor interactions with platelets. Interdependence of glycoproteins Ib and IIb/IIIa for binding and aggregation.

Grainick¹,

Williams²,

Coller³

1985

J. Clin. Invest.

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Asialo von Willebrand factor (AS-vWf) binds to and aggregates normal human platelets in the absence of ristocetin. Maximal specific binding of AS-vWf is 1-2 ug vWf protein/108 platelets.Despite the specificity of the binding, only 60% of the bound AS-vWf can be dissociated after equilibrium has been reached. We investigated the site of binding and the mechanism of aggregation of platelets by AS-vWf by (a) pre-incubating platelets with either of two monoclonal antibodies, one against glycoprotein lb (GPIb) to normal primary hemostasis, that is, the adhesion of platelets to subendothelial surfaces and the subsequent aggregation of platelets (1, 2). Human vWf in the presence of ristocetin binds to the glycoprotein lb (GPIb) of platelets that are either intact metabolically or have been fixed with formaldehyde. To date, no in vivo analogue of ristocetin has been found. DeMarco and Shapiro reported, however, that asialo vWf (AS-vWf) binds spontaneously and independently of ristocetin to the platelet surface and causes aggregation (3). They postulated that this represented a possible mechanism for the in vivo binding of vWf to human platelets and subsequent adhesion and aggregation.We have undertaken an investigation to determine the site or sites of AS-vWf binding to human platelets, the effects of other plasma proteins on the binding, and the mechanism(s) of platelet aggregation induced by AS-vWf. Our studies employed (a) monoclonal antibodies specific for GPIb and the glycoprotein lIb/Ila complex (GPIIb/IIIa), (b) plasmas containing variable concentrations of fibrinogen, and (c) the platelets from thrombasthenic patients. MethodsBlood was drawn from normal subjects and patients by use of a twosyringe technique. A 19-gauge needle was used and the initial 5-10 ml of blood was used for other laboratory tests. The blood from the second syringe was placed into polypropylene tubes containing 0.1 ml sodium citrate anticoagulant, final concentration 10.9 mM. Plateletrich plasma (PRP) was prepared from whole blood by removal of the plasma-platelet layer after centrifugation at 750 relative centrifugal force (RCF) for 3 min at 250C. In some experiments, the platelets were washed free of erythrocytes and leukocytes by the preparation of PRP and one wash of the erythrocytes with Hepes buffer, pH 7.35 (4). The PRP and wash were then placed on a discontinuous arabinogalactan gradient 20% (3 ml) and 10% (5 ml) and platelets were separated from plasma proteins by centrifugation at 2,000 RCF for 30 min. The platelets (>85% recovery) were then resuspended in autologous or homologous normal plasma or plasma from two patients with congenital afibrinogenemia. Plasma was obtained from two patients with congenital afibrinogenemia who had thrombin time > 300 s, and no detectable fibrinogen by the Clauss technique or tanned erythrocyte hemagglutination inhibition, i.e., a level < 0.5 isg/ml. Mixing studies were performed to ensure that neither afibrinogenemic plasma contained antifibrinogen antibodies. Each afibrinogenemic plasma...

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Solid state lactoperoxidase: A highly stable enzyme for simple, gentle iodination of proteins

Cited by 247 publications

References 20 publications

Characterization of membrane homing receptors in two cloned murine hemopoietic progenitor cell lines.

Characterization of membrane homing receptors in two cloned murine hemopoietic progenitor cell lines.

Desialation of transferrin by rat liver endothelium.

Asialo von Willebrand factor interactions with platelets. Interdependence of glycoproteins Ib and IIb/IIIa for binding and aggregation.

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