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Biomedical subjects

R F Murphy

Publications and source records attributed to R F Murphy.

At least 235 records · Page 13Linked to original sources
PubMedDate not supplied

Substitution of Ser61----Gly61 in human apolipoprotein C-II does not alter its activation of lipoprotein lipase.

Lipoprotein lipase (LpL) activity is enhanced by apolipoprotein C-II (apoC-II), a 79 amino acid residue peptide. The minimal apoC-II sequence required for activation of LpL resides between residues 56-79. To determine the possible role of an acyl-apoC-II intermediate involving Ser61 in enzyme catalysis, a synthetic peptide of apoC-II containing residues 56-79 was synthesized and compared to the corresponding peptide with serine at position 61 being substituted with glycine. With two different LpL assay systems, both peptides enhanced enzyme activity. Since glycine does not contain a hydroxyl group, these results rule out the possibility that an acyl-apoC-II intermediate with Ser61 is required for enzyme activation.

Amino Acids↗
PubMedDate not supplied

Peptide histidine isoleucine (PHI) immunoreactivity in the rat retina: identification and characterisation by radioimmunoassay, immunohistochemistry and high-performance liquid chromatography.

The presence of peptide histidine isoleucine immunoreactivity (PHI-IR) in the retinae of male Wistar rats has been demonstrated using a specific radioimmunoassay (RIA), immunohistochemistry (IHC) and high performance liquid chromatography (HPLC). PHI levels (mean +/- S.E.M.) of 16.68 +/- 1.61 ng/g wet weight of normal retinal tissue were measured by RIA. IHC showed PHI-IR to be localized to a population of amacrine cells distributed along the proximal aspect of the inner nuclear layer and to processes in laminae I and IV of the inner plexiform layer. PHI-IR in retinal extracts was shown to coelute with a synthetic porcine PHI standard on a reverse phase HPLC system. Additionally levels of PHI-IR were significantly increased (P less than 0.001) with light adaptation.

Adaptation, Ocular↗