Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the human circulation, the insulin-like growth factors (IGFs) circulate as part of a growth hormone-dependent 125- to 150-kDa complex. This complex has been postulated to contain, in addition to IGFs and one or more IGF-binding proteins, an acid-labile subunit (ALS) which does not itself bind IGFs. In this study, the ALS has been purified 1600-fold from human serum, and its binding properties have been examined. Fresh serum was fractionated on DEAE-Sephadex, and active fractions (determined by radioimmunoassay) were purified by affinity chromatography on an IGF-agarose column saturated with the plasma IGF-binding protein BP-53. After further high performance anion exchange chromatography, an ALS preparation was obtained which contained only an 84-86-kDa protein doublet, converting to a single 70-kDa band on N-glycanase treatment, and having an amino-terminal sequence unrelated to IGF-binding proteins or receptors. Pure ALS formed a complex with BP-53 (Ka approximately 5 x 10(8) M-1), immunoprecipitable by anti-BP-53 antiserum, only in the presence of IGF-I or IGF-II. This complex appeared at approximately 150 kDa on high performance gel chromatography. Pure ALS had no intrinsic IGF-binding activity and no effect on the binding of IGF-I or IGF-II to BP-53. These studies suggest that formation of the high molecular weight IGF-binding protein complex requires ALS, BP-53, and IGF.
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PMID:High molecular weight insulin-like growth factor binding protein complex. Purification and properties of the acid-labile subunit from human serum. 247 65

The growth hormone receptor (GHR) cDNA was cloned from the liver of soft-shelled turtle (Pelodiscus sinensis japonicus) using the polymerase chain reaction (PCR). Although GHR has been cloned from several mammalian and avian species, this is the first description of the reptilian receptor. As deduced from the nucleotide sequence, the precursor GHR of soft-shelled turtle (tGHR) is a protein of 615 amino acids which presents 72% identity with the chicken receptor and 57-64% identity with GHRs of several mammals. The tGHR expressed in COS-7 cells specifically bound human growth hormone (hGH) and was able to transduce an activation of transcription in the transfected cells. Binding of (125)I-hGH to the expressed receptor was decreased by the addition of excess unlabeled hGH, pig GH, and bream GH but not by pig insulin. The open reading frame of tGHR cDNA was inserted into the pSINrep/gfp (green fluorescence protein) vector and the tGHR-gfp fusion protein was stably expressed in baby hamster kidney (BHK) cells. Confocal imaging showed that tGHR-gfp was largely concentrated on the plasma membrane. Western blot analysis and deglycosylation treatment with PNGase F demonstrated that tGHR was a glycoprotein in BHK cells.
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PMID:cDNA cloning and functional expression of growth hormone receptor from soft-shelled turtle (Pelodiscus sinensis japonicus). 1101 74