دورية أكاديمية
Identification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound protein.
| العنوان: | Identification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound protein. |
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| المؤلفون: | To WY; Department of Medicine, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin., Leung JC, Lai KN |
| المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 1995 May 18; Vol. 1249 (1), pp. 58-64. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
| مواضيع طبية MeSH: | Plant Lectins*, Blood Proteins/*chemistry , Lectins/*chemistry, Amino Acid Sequence ; Blood Proteins/isolation & purification ; Chromatography, Affinity ; Humans ; Immunoglobulin A/chemistry ; Immunoglobulin A/isolation & purification ; Molecular Sequence Data ; alpha-2-HS-Glycoprotein |
| مستخلص: | We recently adopted immobilized jacalin as an affinity adsorbent to purify human serum IgA for laboratory study. In the course of our investigation, we detected a serum protein that co-eluted with IgA from jacalin-agarose affinity column. It constituted in significant quantity (24.0 +/- 0.9%, n = 30) of total jacalin-bound protein (JBP) and the yield was equivalent to 0.4 +/- 0.1 mg per ml serum. The molecular mass of this protein was 55 kDa with electromobility in the alpha 2 region as demonstrated by SDS-PAGE and immunoelectrophoresis. N-terminal microsequencing of this 55 kDa protein revealed that it is human alpha 2-HS glycoprotein (alpha 2HSG). The molecular interaction of alpha 2HSG with jacalin was characterized by competitive ELISA: human serum IgA, human colostrum secretory IgA (sIgA), and monosaccharides including D-galactose and melibiose exhibited strong inhibitory effect on its binding to jacalin. Accordingly, we propose that human alpha 2HSG binds in a similar manner as that of the bovine fetuin to jacalin. In addition, alpha 2HSG displays similar binding property to jacalin from different geographic area (India and Malaysia) and from different laboratory preparations (Sigma, Pierce and 'homemade' jacalin). |
| المشرفين على المادة: | 0 (AHSG protein, human) 0 (Blood Proteins) 0 (Immunoglobulin A) 0 (Lectins) 0 (Plant Lectins) 0 (alpha-2-HS-Glycoprotein) 0 (jacalin) |
| تواريخ الأحداث: | Date Created: 19950518 Date Completed: 19950705 Latest Revision: 20190610 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/0167-4838(95)00063-z |
| PMID: | 7766684 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0006-3002 |
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| DOI: | 10.1016/0167-4838(95)00063-z |