A comparative study of horseradish peroxidase conjugates prepared with a one-step and a two-step method.

Boorsma, D. M.; Kalsbeek, G.L.

doi:10.1177/23.3.47869

Cited by 73 publications

(20 citation statements)

References 18 publications

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“…The C 1 fragment was conjugated to horseradish peroxidase (HRP) by the two-step method using a bifunctional reagent (14). The conjugate was purified using high-pressure liquid chromatography (TSK 3000 column).…”

Section: Peroxidase Conjugation and Histologic Localizationmentioning

confidence: 99%

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Characterization of a laminin receptor from human breast carcinoma tissue

Barsky

Rao

Hyams

et al. 1984

Breast Cancer Res Tr

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Human breast carcinoma contains high-affinity receptors for the basement membrane glycoprotein laminin. Plasma membranes isolated from tissue samples of human breast carcinoma exhibit specific, saturable, reversible, and displaceable binding to laminin. Fibronectin, collagen, and serum proteins fail to displace this bound laminin. Scatchard analysis is linear with a Kd of 1.8 X 10(-9) M. The laminin receptor, isolated and purified 1200-fold by laminin-affinity chromatography, exhibits a molecular weight of 67 000 daltons as determined by gel electrophoresis. The receptor was verified to be located on the cell surface of the invading breast carcinoma cells by immunohistologic studies utilizing a peroxidase-conjugated fragment of the laminin molecule which contained the receptor-binding domain.

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Section: Peroxidase Conjugation and Histologic Localizationmentioning

confidence: 99%

“…Competition for binding was verified histologically using 1 mg/ml of laminin or the C~ fragment. Peroxidase activity was localized using 3,3'-diaminobenzidine: H202 (1,14).…”

Section: Peroxidase Conjugation and Histologic Localizationmentioning

confidence: 99%

Characterization of a laminin receptor from human breast carcinoma tissue

Barsky

Rao

Hyams

et al. 1984

Breast Cancer Res Tr

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“…Peroxidase (Boehringer, Mannheim, FRG) was coupled to anti-C3 IgG with glutaraldehyde in a two-step procedure as described by Boorsma et al [21]. Purified peroxidase-labeled anti-C3 IgG was diluted in potassium phosphate 10 mM, pH 7.5, with the addition of NaCl to a conductivity of 15 mS (15 mS NaCl), 1% BSA, to be in excess for the detection of 100 ng C3/ml.…”

Section: Assay For Gp C3mentioning

confidence: 99%

Quantitative studies of the secretion of complement component C3 by resident, elicited and activated macrophages. Comparison with C2, C4 and lysosomal enzyme release

Zimmer¹,

Hartung²,

Scharfenberger³

et al. 1982

Eur J Immunol

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To quantitate the secretion of complement component C3 by guinea pig peritoneal macrophages an enzyme-linked immunosorbent assay was developed. C3 secretion was studied in resident, elicited and activated macrophages and compared with release of hemolytically active C2 and C4, as well as the lysosomal enzyme beta-D-2-acetamido-2-deoxyglucosidase. Resident macrophages secreted about 6 ng C3/10(6) cells/h into culture supernatants over a period of 12 h. Corynebacterium parvum-activated cells were found to secrete 3 times that amount at nearly constant rates. There was a stepwise increase in secretion of functional C2 and C4 when comparing resident, elicited and activated macrophages; secretion was 2--4 times higher in activated than in resident cells.

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“…I ml 0.2 M lysine. The IgG-HRPO conjugate was separated from free IgG and HRPO on a Sephacryl S-200 Superfine column (1.6 • 100 cm) eluted with PBS buffer, pH 7.2, at a flow rate of 4 ml/h [25]. The IgG-HRPO conjugate was stored frozen in portions of 0.5 ml at -22~ prior to the immunohistochemical experiments.…”

Section: Hrpo Conjugationmentioning

confidence: 99%

Cathepsin D: Ultra-immunohistochemical localization in dentinogenesis

Nygren

Persliden

et al. 1979

Calcif Tissue Int

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Cathepsin D was purified from rat liver using a new affinity chromatographic method, based on the coupling to the specific inhibitor pepstatin. This preparation was used for the production of specific antibodies from rabbit. The purified IgG fraction was conjugated to horseradish peroxidase in a two-step coupling procedure and used for electron microscopic immunohistochemistry of the odontoblast-predentine region of the rat incisor. Precipitates, indicating the presence of cathepsin D, were seen in the odontoblast, odontoblast process, and in the extracellular unmineralized matrix, the predentine. The observations are discussed in relation to proteoglycan degradation at the mineralization front simultaneous with crystal formation, and in relation to the function of lysosomal enzymes in the turnover of connective tissue.

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A comparative study of horseradish peroxidase conjugates prepared with a one-step and a two-step method.

Cited by 73 publications

References 18 publications

Characterization of a laminin receptor from human breast carcinoma tissue

Characterization of a laminin receptor from human breast carcinoma tissue

Quantitative studies of the secretion of complement component C3 by resident, elicited and activated macrophages. Comparison with C2, C4 and lysosomal enzyme release

Cathepsin D: Ultra-immunohistochemical localization in dentinogenesis

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