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Histamine binding proteins separated from human sera by the chromatographic method
Archivum Immunologiae Et Therapiae Experimentalis
|January 1, 1980
Summary
Researchers identified three histamine-binding protein fractions in human serum using affinity chromatography. One fraction was orosomucoid, with two others identified as alpha-1 globulin glycoproteins, aiding in understanding histamine interactions.
Area of Science:
- Biochemistry
- Immunology
Background:
- Histamine is a crucial biogenic amine involved in various physiological processes.
- Understanding the binding proteins for histamine in human serum is essential for comprehending its regulation and function.
Purpose of the Study:
- To isolate and characterize histamine-binding proteins (HBP) from human serum.
- To identify the specific serum protein fractions responsible for histamine binding activity.
Main Methods:
- Affinity chromatography using a sepharose-polylysine-histamine column to isolate HBP.
- Biological assay on isolated guinea pig intestine to confirm histamine-binding capacity.
- DEAE ion-exchange chromatography to further purify and identify active fractions.
Main Results:
- Three distinct histamine-binding protein fractions were successfully isolated from human serum.
- One identified fraction was orosomucoid (alpha-1-acid glycoprotein).
- The remaining two fractions were characterized as glycoproteins belonging to the alpha-1 globulin group.
Conclusions:
- Human serum contains multiple protein components capable of binding histamine.
- Orosomucoid and other alpha-1 globulin glycoproteins play a significant role in serum histamine binding.
- These findings contribute to the understanding of histamine metabolism and transport in biological systems.