Why does the clicking temporomandibular joint not lock, and the locked joint not click. Why is either of these conditions painful? Improved temporomandibular joint arthrography is able to delineate the problem and to direct surgical intervention appropriately, rather than toward the empirical remedies of the recent past.

Humans↗

PubMed1983

The use of arthrography in management of temporomandibular joint problems.

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Adolescent↗

PubMed1983

Effects of kallikrein on human platelet aggregation.

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Adenosine Diphosphate↗

PubMed1982

The role of translational inhibitor in ethionine-induced inhibition of protein synthesis.

The soluble fraction from rat liver contains an inhibitor of protein chain initiation when tested in a cell-free protein-synthesizing system derived from rabbit reticulocytes. The administration of ethionine to rats increased the inhibitory activity in the liver. This liver inhibitor displayed properties similar to those of hemin-controlled inhibitor found in rabbit reticulocytes: (i) the liver inhibitor inhibited protein chain initiation in rabbit reticulocyte lysate with characteristic biphasic kinetics; (ii) the liver inhibitor disaggregated the reticulocyte polysomes with a concomitant increase in 80 S ribosomes; (iii) the inhibition was prevented or reversed by eIF-2. The activation of the liver inhibitor by ethionine was rapidly and completely counteracted by the subsequent administration of methionine and adenine to rats. The mechanism of inhibition of protein synthesis by ethionine was discussed in the light of these findings.

Animals↗

PubMed1982

A cell-free system from ethionine-treated rat liver active in initiation of protein synthesis.

A cell-free protein-synthesizing system active in initiation of translation of both endogenous mRNA and exogenous mRNA has been obtained from postmitochondrial supernatant (S-12) of the liver of ethionine-treated rats by adding reticulocyte ribosomal extract as a source of initiation factor. Formation of polysomes in the course of protein synthesis in vitro has also been demonstrated. Homogenization of the liver in the presence of 50 microM hemin stabilizes the initiation activity of S-12 fraction, which otherwise decays rapidly even at 0 degrees C. The mechanism of inhibition of protein synthesis by ethionine is discussed in view of these results.

Animals↗

PubMed1982