Chemie und Funktion der Human-Plasmaproteine

Schwick, H. G.; Haupt, H.

doi:10.1002/ange.19800920205

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Evidence For the Igci Nature Of The Ap-hinding Proteins1

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1981

1996

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Cited by 14 publications

(2 citation statements)

References 88 publications

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“…In other studies, Schousboe (10,11) has presented evidence that 1321 specifically binds to platelet membranes and modulates the activity of adenylate cyclase. 121 is precipitated by heparin and transports heparin in agar gel electrophoresis (12). However, the above research has not yet provided a clear determination of the role of 132I in normal human metabolism.…”

mentioning

confidence: 99%

Complete amino acid sequence of human plasma beta 2-glycoprotein I.

Lozier¹,

Takahashi²,

Putnam³

1984

Proc. Natl. Acad. Sci. U.S.A.

329

223

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mentioning

confidence: 99%

Complete amino acid sequence of human plasma beta 2-glycoprotein I.

Lozier¹,

Takahashi²,

Putnam³

1984

Proc. Natl. Acad. Sci. U.S.A.

329

223

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“…Upon IEF IgG is evenly distributed in the cationic range where tlie AP-binding pattern islocalized.Only a very few other serum proteins with alkaline isoelectric points (pi) are known [12]. The following experimenls were conducted to elucidate whether the AP-binding proteins were truly IgG: serum IgG of one patient was purified on protein A Sepharose and subsequently separated using IEF.…”

Section: Evidence For the Igci Nature Of The Ap-hinding Proteinsmentioning

confidence: 99%

Human intestinal alkaline phosphatase-binding IgG in patients with severe bacterial infections

Mäder¹,

Kolbus²,

Meihorst³

et al. 1994

Clinical and Experimental Immunology

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SUMMARYPatterns of alkaline phosphalase (AP)-binding proteins were observed in the alkaline pH range of 6-5-9-5 upon isoclcctric focusing and blotling of serum from patients with inflammalory diseases. Afler isolation using affinity chromatography on prolein A or immunoaffinity chromatography on AP coupled to cyanogen bromide (CNBr)-activaled Sepharose. the AP-binding protein was identified as IgG on Western blols and in ELISA using human igG-specilic aniibodies. It was shown thai this IgG binds to AP from both calf (bovine) and human intestine. However, it binds neither lo the human liver-bone-kidncy (LBK) isoform nor to bacterial AP. Moderate reaction was observed with human placental AP. Comparing patients with various diagnoses (H = 284), AP-binding antibodies were mainly found in severe bacterial infections. They were not detected in serum from healthy blood donors (rt = 3()0). The presence of AP-binding IgG was independent of the infeeled organ and the bacterial species causing infection. This antibody may be useful for discriminating bacteria! from viral infection and for indicating severe bacterial inflammation.

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Zur möglichen Funktion von Sekundärstoffen in biologischen Systemen

Teuscher¹

1984

Biogene Arzneistoffe

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Chemie und Funktion der Human-Plasmaproteine

Cited by 14 publications

References 88 publications

Complete amino acid sequence of human plasma beta 2-glycoprotein I.

Complete amino acid sequence of human plasma beta 2-glycoprotein I.

Human intestinal alkaline phosphatase-binding IgG in patients with severe bacterial infections

Zur möglichen Funktion von Sekundärstoffen in biologischen Systemen

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