Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tests commonly used to assess the glomerular filtration rate (GFR) and to detect renal tubular damage are critically reviewed. Creatinine clearance which is frequently used for assessment of the GFR is prone to several errors. The plasma creatinine can be used to provide a rough guide but for reliable measurement of the GFR, 51Cr-EDTA clearance is recommended. Measurements of the urinary excretion of low molecular weight proteins, enzymes and kidney tissue proteins have been used to detect tubular damage. Of the low molecular weight proteins excreted, beta-2-microglobulin is unstable and measurement of retinol-binding protein or alpha-1-microglobulin is recommended for the detection of chronic renal tubular malfunction. Of the many enzymes that have been studied, urinary N-acetyl-beta-D-glucosaminidase or alanine aminopeptidase are recommended as being the most useful for the early detection of acute renal tubular damage. Among renal tissue proteins that have been measured in urine adenosine-deaminase-binding protein, a tubular brush border antigen appears to have considerable potential for providing early warning of renal allograft rejection.
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PMID:Assessment of renal function: selected developments. 218 56

The mature form of human protein HC, or alpha 1-microglobulin, has been expressed in Escherichia coli. Protein HC is a member of the lipocalin superfamily of hydrophobic ligand-binding proteins, and carries a heterogeneous chromophore linked covalently by a reduction-resistant bond. Protein HC was first overexpressed as a C-LytA/HC fusion protein containing the C-terminal moiety of the pneumococcal lytic amidase (LytA). Recombinant C-LytA/HC was found to be an insoluble aggregate that was solubilized with 6 M guanidinium chloride and renatured by the addition of thiol reagents in the presence of L-arginine. Recombinant protein HC (rHC) was released from C-LytA/HC by trypsin digestion and purified by size-exclusion chromatography. rHC protein possesses an N-terminal amino-acid sequence identical to that of human protein HC, and a slightly lower molecular mass as determined by SDS-PAGE. Both C-LytA/HC and rHC reacted with polyclonal antibodies raised against native protein HC. A photodiode array detection system on-line with a HPLC system has allowed the identification of a chromophore associated to rHC protein displaying significant absorption in the visible region of the spectrum in resemblance to that found in the natural form of human protein HC.
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PMID:Expression of the human complex-forming glycoprotein HC (alpha 1-microglobulin) in Escherichia coli. 753 95