Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the present study, it is shown that the pattern of the isoelectric focusing with immunofixation changes markedly in the presence of substances such as platelet extract, trypsin, chymotrypsin, vitamin D3 and neuraminidase. It has been recently found that the factor of platelet extract is actin (K. Shinomiya et al., Jpn. J. Legal Med., 36 (1982) 542-549; J. Biochem., 92 (1982) 1163-1171), and Gc globulin is bound by actin (H. Van Baelen et al., J. Biol. Chem., 255 (1980) 2270-2272). The Gc-actin complex appeared as supplementary bands of Gc-globulin near by the anode band of Gc1F-1F or Gc1S-1S. As to the Gc2-2, the supplementary band of Gc-actin complex appeared on the cathode side of the original anode band of Gc1F-1F or Gc1S-1S. Concerning Gc1F-1F (or Gc1S-1S), two supplementary bands of Gc-actin complex appeared on the anode side of the original band. Each product originated from the digestion of Gc-globulins of common phenotypes by trypsin appeared as four characteristic bands on the anode side of the original band. On the other hand, each product obtained by treatment of Gc-globulins of common phenotypes with chymotrypsin appeared as two characteristic bands on the anode side near the anode band of Gc1F-1F. The results obtained in this study give useful information to distinguish the pattern between original and supplementary bands which were altered by the action of factors.
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PMID:[Influence of the factors altering the electrophoretic migration of the alpha 2 Gc globulin in the diagram of iso-electric focusing of the Gc type]. 654 Nov 79

Vitamin D-binding protein (DBP), a multi-functional serum glycoprotein, has a triple-domain modular structure. Mutation of Trp145 (in Domain I) to Ser decreased 25-OH-D(3)-binding by 80%. Furthermore, recombinant Domain I (1-203) and Domain I + II (1-330) showed specific and strong binding for 25-OH-D(3), but Domain III (375-427) did not, suggesting that only Domains I and II might be required for vitamin D sterol-binding. Past studies have suggested that Domain III is independently capable of binding G-actin. We exploited this apparently independent ligand-binding property of DBP to purify DBP-actin complex from human serum and rabbit muscle actin by 25-OH-D(3) affinity chromatography. Competitive (3)H-25-OH-D(3) binding curves for native DBP and DBP-actin complex were almost identical, further suggesting that vitamin D sterol- and actin-binding activities by DBP might be largely independent of each other. Trypsin treatment of DBP produced a prominent 25 kDa band (Domain I, minus 5 amino acids in N-terminus), while actin was completely fragmented by such treatment. In contrast, tryptic digestion of purified DBP-actin complex showed two prominent bands, 52 (DBP, minus 5 amino acids in the N-terminus) and 34 kDa (actin, starting with amino acid position 69) indicating that DBP, particularly its Domains II and III were protected from trypsin cleavage upon actin-binding. Similarly, actin, except its N-terminus, was also protected from tryptic digestion when complexed with DBP. These results provided the basis for our studies to crystallize DBP-actin complex, which produced a 2.5 A crystal, primitive orthorhombic with unit cell dimensions a=80.2A, b=87.3A, and c=159.6A, P2(1)2(1)2(1) space group, V(m)=2.9. Soaking of crystals of actin-DBP in crystallization buffer containing various concentrations of 25-OH-D(3) resulted in cracking of the crystal, which was probably a reflection of a ligand-induced conformational change in the complex, disrupting crystal contacts. In conclusion, we have provided data to suggest that although binding of 25-OH-D(3) to DBP might result in discrete conformational changes in the holo-protein to influence actin-binding, these binding processes are largely independent of each other in solution.
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PMID:Biochemical and preliminary crystallographic characterization of the vitamin D sterol- and actin-binding by human vitamin D-binding protein. 1205 78

To identify acute renal allograft rejection biomarkers in human serum, two-dimensional differential in-gel electrophoresis (2-D DIGE) and reversed phase high-performance liquid chromatography (RP-HPLC) followed by electrospray ionization mass spectrometry (ESI-MS) were used. Serum samples from renal allograft patients and normal volunteers were divided into three groups: acute rejection (AR), stable renal function (SRF) and normal volunteer (N). Serum samples were firstly processed using Multiple Affinity Removal Column to selectively remove the highest abundance proteins. Differentially expressed proteins were analyzed using 2-D DIGE. These differential protein spots were excised, digested by trypsin, and identified by RP-HPLC-ESI/MS. Twenty-two differentially expressed proteins were identified in serum from AR group. These proteins included complement C9 precursor, apolipoprotein A-IV precursor, vitamin D-binding protein precursor, beta-2-glycoprotein 1 precursor, etc. Vitamin D-binding protein, one of these proteins, was confirmed by ELISA in the independent set of serum samples. In conclusion, the differentially expressed proteins as serum biomarker candidates may provide the basis of acute rejection noninvasive diagnosis. Confirmed vitamin D-binding protein may be one of serum biomarkers of acute rejection. Furthermore, it may provide great insights into understanding the mechanisms and potential treatment strategy of acute rejection.
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PMID:Characterization of acute renal allograft rejection by human serum proteomic analysis. 1982 Oct 91