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H Loh

Publications and source records attributed to H Loh.

27 records · Page 2Linked to original sources
PubMed1976

Physical dependence of opiate-like peptides.

Methionine-enkephalin and beta-endorphin, endogenous peptides with activities similar to those of opiates, were infused for 70 hours into the periaqueductal gray-fourth ventricular space of the rat brain. When challenged with a naloxone, a specific opiate antagonist, these animals manifested a typical morphine-like withdrawal syndrome. These results show that such peptides can cause physical dependence.

Animals↗
PubMed1976

Potency of the N3im-methyl analog of TRH in the induction of shaking movements in the rat.

The relative potencies of TRH analogs in provoking a shaking response in rats were determined. Bilateral administration of 0.011-2.0 mug TRH analog into the periaqueductal-fourth ventricular spaces of the barbiturate-anesthetized rat showed that N3im-methyl TRH was approximately 10X more potent than TRH, whereas N1im-methyl TRH was approximately 10X less potent than TRH. These results indicate that the potencies of the TRH analogs in inducing shaking parallel their thyrotropin-releasing activities.

Animals↗
PubMedDate not supplied

Immunoreactive peptides related to dynorphin B (= rimorphin) in the rat brain.

We have developed a radioimmunoassay for synthetic dynorphin B, a novel opioid tridecapeptide, which shares a common precursor molecule with dynorphin1-17 (= dynorphin A) and the neo-endorphins. The levels of immunoreactivity towards this peptide in rat brain and pituitary show a pattern quantitatively and qualitatively similar to those found for dynorphin A and alpha-neo-endorphin in earlier studies. The antiserum used was highly specific with only dynorphin-32 and dynorphin B-29, both of which contain the dynorphin B sequence, showing substantial cross-reactivity. Gel filtration of whole rat brain extracts in combination with HPLC analysis provide strong evidence for the existence of these latter two peptides in rat brain.

Animals↗
PubMedDate not supplied

Detection and screening of Salmonella enteritidis-infected chickens with recombinant flagellin.

Screening and identification of Salmonella enteritidis in commercial poultry flocks have assumed principal roles in preventing transmission of this pathogen to humans from hen eggs. Serologic diagnosis of S. enteritidis infection in commercial flocks currently relies on laboratory-based tests for detection of antibodies to the lipopolysaccharide, whole flagella, and bacteria. We amplified a sequence from the g,m flagellin of S. enteritidis, followed by cloning, expression, and purification of the protein. The recombinant protein was first characterized by western blot and subsequently evaluated as enzyme-linked immunosorbent assay (ELISA) antigen for detection of S. enteritidis infection. A total number of 49 positive sera and 40 negative sera were tested for ELISA validation. A cutoff value of 0.14 was shown to be sufficient to discriminate the negative and positive sera. Results obtained by testing sera raised against different bacterial strains/serotypes further confirmed that this recombinant flagellin-based ELISA was indeed specific for the detection of S. enteritidis. Both sensitivity and specificity of the developed ELISA test were comparable with a commercially available test, indicating that it is a highly promising and reliable diagnostic tool for S. enteritidis infection.

Animals↗