Assessment of specificity of antisera for immunohistochemistry.

Wakabayashi, Keiji; Tanaka, Shigeyasu

doi:10.1267/ahc.21.221

Cited by 29 publications

(16 citation statements)

References 8 publications

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“…The working dilution of TSH S-1 used for immunostaining was 1:2000 and that of the anti-TSH serum was 1:15000-1:25000. The specificity of the antibody has been described elsewhere (KAWARAI, 1980;WAKABAYASHI and TANAKA, 1988).…”

Section: Light Microscopic Immunocytochemistrymentioning

confidence: 99%

Light and Electron Microscopic Immunocytochemistry of TSH-like Cells Occurring in the Pars tuberalis of the Adult Male Rat Pituitary.

Sakai

Inoue

Kurosumi

1992

Archives of Histology and Cytology

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Section: Light Microscopic Immunocytochemistrymentioning

confidence: 99%

Light and Electron Microscopic Immunocytochemistry of TSH-like Cells Occurring in the Pars tuberalis of the Adult Male Rat Pituitary.

Sakai

Inoue

Kurosumi

1992

Archives of Histology and Cytology

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“…On the other hand, the affinity of fraction B with canine motilin was lower than that [3] attributed these phenomena to the affinity of the antibody with the antigen and explained by means of simulation that antisera with low affinity which can never be used in RIA were successfully employed in immunohistochemical staining when the concentrations of the antibodies were satisfactorily high. This explanation seems applicable mainly to monoclonal antibodies which have homogeneous binding specificity and affinity with antigens.…”

Section: Discussionmentioning

confidence: 98%

Radioimmunoassay with Heterologous Antibody(Hetero-Antibody RIA): Utilization of Highly Cross-Reactive Antibody Present in Polyclonal Antiserum.

1991

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“…The LH level was determined by double antibody RIA [16], with an NIDDK assay kit (NIDDK LH I-9 for radioiodination, NIDDK LH RP-3 as the standard and NIDDK anti-LH S-11 as the antiserum) with the 2nd antibody prepared in our laboratory (HAC-RBA2-03GTP86). The sensitivity and intra-and inter-assay coefficients of variation were 0.125 ng/ml, 4.77% and 6.01%, respectively.…”

Section: Radioimmunoassaymentioning

confidence: 99%

In Vivo Bioactivities and Kinetic Parameters of Rat Luteinizing Hormone Components: Discrepancy Between In Vivo and In Vivo Assays.

Shioya

Wakabyashi

1998

Endocr J

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Abstract.Rat pituitary LH shows an electrical charge heterogeneity owing to their carbohydrate moiety. The biological potencies of these isoelectric components increase with increasing pi when examined by in vitro testosterone production in isolated rat Leydig cells. The present study was carried out to clarify if this tendency was also true with of in vivo action and to estimate their kinetic parameters. Seven isoelectric components of LH, i.e. X (pI 7.9), A (8.4), B (8.8), C (9.1), D (9.3), E (9.6) and F (9.8), were administered to cannulated adult male rats. Blood samples were serially collected over a 5 h period from the conscious animal, and rat LH and testosterone were assayed by RIA. The doses of a single component showed a linear relationship with the areas under the curve (AUC) of the blood LH. The testosterone AUC also correlated well with LH AUC. It was found that the components with lower pls had longer half-lives and larger LH AUC, and smaller total body clearance rates with highly significant correlation coefficients.The in vivo bioactivities of the components expressed as testosterone AUC increased with decreasing pIs, indicating that the in vivo bioactivity was much influenced by the total body clearance rate. The intrinsic activities of the components were calculated as ratios of testosterone AUC to LH AUC where the effect of the clearance rate (or biological half-life) was eliminated. The intrinsic activities of components were not significantly different among the components except component X which showed a smaller activity. These data indicated that, with the exception of component X, an LH component with a lower pI has a longer biological half-life, resulting in a higher in vivo potency, quite contrary to the tendency of in vitro potency.Key words: Charge heterogeneity, Rat LH, In vivo activity (Endocrine Journal 45: 307-314,1998) LH is a glycoprotein hormone consisting of two non-covalently linked subunits, a and f3. The asubunit contains two N-linked oligosaccharides, and the fl-subunit contains one such oligosaccharide [1]. Depending on the differences in isoelectric points (pls), rat pituitary LH can be separated into

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Assessment of specificity of antisera for immunohistochemistry.

Cited by 29 publications

References 8 publications

Light and Electron Microscopic Immunocytochemistry of TSH-like Cells Occurring in the Pars tuberalis of the Adult Male Rat Pituitary.

Light and Electron Microscopic Immunocytochemistry of TSH-like Cells Occurring in the Pars tuberalis of the Adult Male Rat Pituitary.

Radioimmunoassay with Heterologous Antibody(Hetero-Antibody RIA): Utilization of Highly Cross-Reactive Antibody Present in Polyclonal Antiserum.

In Vivo Bioactivities and Kinetic Parameters of Rat Luteinizing Hormone Components: Discrepancy Between In Vivo and In Vivo Assays.

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