Conformation and sequence dependent antigenic determinants in human low molecular weight kininogen

Syvänen, Ann‐Christine; Kärkkäinen, Tytti; Hamberg, Ulla

doi:10.1016/0161-5890(83)90011-1

Cited by 5 publications

(4 citation statements)

References 23 publications

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“…The low-A4* kininogen occurs in several immunoreactive isoelectric forms with the main component at pZ 4.5-4.6 and that of high-M, kininogen at pZ 4. 7 however, identical isoelectric patterns [6]. This indicates that the lectin-binding heterogeneity is not charge dependent.…”

Section: Introductionmentioning

confidence: 83%

“…Antiserum against HC antigen was prepared in rabbits using the immunologically pure antigen containing the conformation-dependent determinants of the native kininogen [7]. The association constant of this antiserum against the native kininogen was 3.8 x lo9 M-'.…”

Section: Preparation Of Antiserummentioning

confidence: 99%

“…The radioiodinated protein was diluted 1: 10 in 50 mM sodium phosphate buffer, pH 7.5, containing 0.25% bovine albumin, 0.15 M NaCl and 0.01% NaN3 and stored at -70°C. The antiserum was diluted 1:20000 in the same buffer for RIA [7,12].…”

Section: Riamentioning

confidence: 99%

“…Exoglycosidase treatments, addition of carbohydrates and chemical modifications are performed. The antigenicity of the protein is measured by radioimmunoassay (RIA) using antisera against the conformational determinants of HC antigen [7].…”

Section: Introductionmentioning

confidence: 99%

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The role of carbohydrates in the radioimmunoassay of human low‐molecular‐mass kininogen

Turpeinen

Kärkkäinen

1985

FEBS Letters

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The immunoreactivity of human low-molecular-mass kininogen from Cohn plasma fraction IV was investigated after deglycosylations and carbohydrate modifications by radioimmunoassay using the conformationspecific antiserum. Removal of all sialic acids, 44% of amino sugars and 63% of neutral sugars did not alter the immunoreactivity of the protein but the periodate-treated concanavalin A fractions showed strikingly diminished immunoreactivity. A conformational change could account for the observed effect of periodate on the decreased reactivity of the protein in radioimmunoassay. Externally added carbohydrates had no effect on immunoreactivity. The results suggest that the carbohydrate part of kininogen is not involved in the immunoreactivity although it accounts for the observed lectin-binding heterogeneity.Carbohydrate Glycoprotein Kininogen

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Section: Introductionmentioning

confidence: 83%

Section: Preparation Of Antiserummentioning

confidence: 99%

Section: Riamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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