The effects on thermoregulation of intracerebroventricular injections of L-aspartic acid in the sheep

Summary L-Aspartic acid was injected into a lateral cerebral ventricle of the sheep at ambient temperatures between 0° and 40°C. Doses of 100 or 500 nmoles·kg^–1 caused a rise in heat production and/or a decrease in heat loss; rectal temperature rose. Atropine sulphate attenuated or prevented these effects.     

Morphine tolerance in a human neuroblastoma line: Changes in choline acetylase and cholinesterase activities

Zusammenfassung Nachweis der Entstehung einer Morphin-Toleranz und-Dependenz sowie von Veränderungen (Steigerung der Cholinesterase, Verminderung der Cholin-o-Acetyltransferase) von Enzymaktivitäten nach länger dauernden Morphingaben bei Neuroblastom-Kulturen.

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Acknowledgements. This work was supported by grant No. U-2270 from the Health Research Council of the City of New York, a Lucy G. Moses Fellowship and an Irma T. Hirschl Career Scientist Award (to G.M.)     

Renal ammonia production as a model for the study of enzyme adaptation in mammals

Zusammenfassung Chronische Verabreichung von Säure führt zu einer erhöhten Glutaminase-I-Konzentration in der Niere und zu einer gesteigerten Ammoniakausscheidung im Urin. Das ammoniakproduzierende biokatalytische System (Glutaminase I) ist besonders gut zum Studium der Enzymadaptation (Induktion) bei Säugetieren geeignet. Der Stand der Adaptation kann nicht nur durch die Bestimmung der Enzymveränderungen in der Niere, sondern auch durch den Nachweis des Reaktionsproduktes (Ammoniak) im Urin am lebenden Tier beurteilt werden.

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This investigation was supported by a research grant, RG-3795, from the National Institutes of Health, United States Public Health Service.     

Lysozyme activity in the plaice (Pleuronectes platessa L.)

Zusammenfassung Die Untersuchung der Lysozymverteilung im Gewebe des Knochenfischs,Pleuronectes platessa L., ergab, dass das Plasma-Lysozym von Leukozyten abstammt, das Hautschleim-Lysozym dagegen von spezifischen Epidermiszellen.     

Evidence for coexistence of dopamine and CCK in meso-limbic neurones

Vanderhaeghen et al. reported the occurrence of gastrin-like immunoreactivity in the mammalian brain. Subsequent studies have revealed that this immunoreactivity corresponded mainly to the COOH-terminal octapeptide of cholecystokinin (CCK-8), which has a COOH-terminal pentapeptide identical to gastrin. Also, two peptides resembling the NH- and the COOH-terminal tetrapeptide fragments of CCK-8 are present in the central nervous system (CNS). Using COOH-terminal-specific antisera raised to gastrin and/or CCK, the distribution of CCK neurones has been described with immunohistochemical techniques. Although high numbers of cells and nerve terminals are found in cortical areas, the CCK systems are also present in most other parts of the brain and spinal cord. In the CNS, true gastrin molecules, gastrin-17 and gastrin-34 have been located only in the neurohypophysis, hypothalamus and occasionally in the medulla oblongata (unpublished results). We describe here the occurrence of peptides in meso-limbic dopamine neurones in the rat brain. Evidence has also been obtained that mesencephalic dopamine neurones in the human brain contain similar peptides.     

Identification of globular mechanochemical heads of kinesin

Kinesin is a mechanoenzyme which uses energy liberated from ATP hydrolysis to transport particles towards the 'plus ends' of microtubules. The enzyme consists of two polypeptide heavy chains of relative molecular mass (Mr) approximately 110,000-140,000 (110K-140K) plus copurifying light chains; these polypeptides are arranged in a structure consisting of two globular heads attached to a fibrous stalk which terminates in a 'feathered' tail. Here we report that a function-disrupting monoclonal antikinesin, which binds to the 45K fragment of the kinesin heavy chain, recognizes an epitope located towards the N-terminal end of the heavy chain, and decorates the two globular heads lying at one end of the intact molecules (one antibody per head). The results show that the two heavy chains of native kinesin are arranged in parallel, and that the 45K fragments, which display nucleotide-sensitive interactions with microtubules, represent mechanochemical 'heads' located at the N-terminal regions of the heavy chains. Thus, it is likely that the kinesin heads are analogous to the subfragment-1 domains of myosin.