Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.61 (porphobilinogen deaminase)
 637 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Non-immobilised ligand interaction assay (NILIA) by CD spectroscopy provides an excellent technique to study molecular interactions in solution. Here are discussed molecular interactions of several systems that involve hosts and ligands with wide range of molecular sizes. Cytokine rhGM-CSF (14.6 kDa) bound to alpha-chain hGM-CSF receptor fragment (2 kDa, Kd = 35 microM), proline rich peptide (1.5 kDa) bound to fynSH3 domain (8 kDa, Kd = 28 microM), tumour imaging peptide (2 kDa) bound to mucin antigenic fragment (2 kDa, Kd = 20 microM), monoclonal antibody (150 kDa) bound to antigenic protein (120 kDa, Kd = 50 nM). Reconstitution of Cytochrome b5 (Cyt b5) from apo-Cyt b5 and hemin (Kd = 1.6 nM), correct protein folding of reconstituted porphobilinogen deaminase from apo-cofactorless form achieved using the product of the enzyme catalysis, preuroporphyrinogen, rather than porphobilinogen substrate. Competition studies of bound non-chiral drugs diclofenac and diazepam to carrier proteins such as HSA in the presence of fatty acids are few of the examples of the studies carried out by NILIA-CD spectroscopy. The CD changes in either backbone, aromatic side-chains and disulphide regions were used accordingly to screen qualitatively and quantitatively ligand binding in vitro. CD data were fitted by non-linear regression to the general equilibrium reaction of a single-binding site. NILIA-CD is fast compared to NMR, gives information on conformational changes due to interaction, avoids masking of the binding site due to immobilisation and requires no radiolabelling. NILIA-CD is thus an ideal technique for interaction, activity, screening studies.
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PMID:Biomolecules interactions and competitions by non-immobilised ligand interaction assay by circular dichroism. 978 30

Peptidoglycan recognition protein (PGRP) binds to peptidoglycan (PG) or live bacteria and is upregulated by PG. PGRP is a ubiquitous protein involved in innate immunity. Tag7, a novel cytokine, is also induced by bacterial products; tag7 is apoptotic to murine L929 cells in a NF-kappaB-independent manner. Both of these genes are expressed in brain, lymphatic and haematopoietic tissues. We provide evidence that murine PGRP and tag7 encode identical transcripts and have structural relationships to lysozymes. Further, we have cloned the cDNA of rat PGRP and analyzed its expression in brains of sleep-deprived and control rats. The mRNA levels of PGRP/tag7 were measured by RT-PCR and compared to the housekeeping gene porphobilinogen deaminase (PBD). PGRP was constitutively expressed in rat brain. PGRP mRNA was increased by 43% and 17% in the brainstem and hypothalamus, respectively, in sleep-deprived rats compared to controls. The upregulation of PGRP expression by sleep deprivation suggests a role for PGRP in a homeostatic regulation of sleep.
Cytokine 2001 Jan 07
PMID:The cloning of a rat peptidoglycan recognition protein (PGRP) and its induction in brain by sleep deprivation. 1114 37