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M Kutzer

Publications and source records attributed to M Kutzer.

10 recordsLinked to original sources

Basolateral glutarate transport by isolated S2 segments of rabbit kidney proximal tubules.

The properties of tubular glutarate uptake and the coupling to p-aminohippurate (PAH) transport were studied on isolated nonperfused S2 segments of proximal tubules, microdissected from rabbit kidneys without the use of enzymatic agents. Because the tubules were totally collapsed, the tubular glutarate uptake may be assumed to represent the quantity transported across the basolateral membrane. The results show that the S2 segments effectively accumulated 14C glutarate (500 micron). The cell/bath 14C-glutarate concentration ratio reached maximum values of about 20 after a 20-min incubation period. The tubular 14C glutarate accumulation could be markedly depressed by lithium (5 mM) but not by probenecid (1 mM), which, however, inhibited tubular 3H-PAH (1 microM ) uptake. External PAH (0.1 mM) stimulated efflux of 14C-glutarate from S2 segments preloaded with 14C-glutarate (500 microM), and external glutarate stimulated tubular uptake of 3H-PAH (1 microM), providing evidence for glutarate-PAH countertransport in proximal S2 segments. The phorbol ester, phorbol 12-myristate 13-acetate (0.1 microM), did not affect steady-state cell/bath 14C-glutarate concentration ratio nor the initial 14C-glutarate transport rate. Protein kinase C may, therefore, not be a regulator of basolateral glutarate transport in renal S2 proximal tubules.

Animals↗

[Not Available].

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Germany↗

Smooth pursuit eye movements in schizophrenia: influences of neuroleptic treatment and the question of specificity.

The authors investigated smooth pursuit eye movements (SPEMs) in 66 schizophrenic and 40 major affective patients and 39 healthy controls. The results showed significant differences of both patient groups as compared to the controls. Schizophrenics with neuroleptic treatment in the preceding 2 years were significantly more disturbed than the controls, the affective patients and the untreated schizophrenics. Acute neuroleptic medication and neuroleptic treatment of a duration of 4-6 weeks appear not to significantly influence the quality of SPEMs.

Adolescent↗

[Not Available].

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Germany↗

[Not Available].

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Germany↗

Temperature-induced transitions in the conformation of intermediates in the hydrolytic cycle of myosin.

The conformations of the transitory intermediates of the myosin ATPase occurring during the hydrolytic cycle, enzyme without ligand, enzyme-substrate complex and two different forms of enzyme-product complex, have been characterized in terms of numbers and classes of reactive thiol groups based on incorporation of radioactively labeled alkylation reagent. The techniques employed allowed this to be done under steady-state conditions in the presence of high ligand concentrations on intact myosin from rabbit fast skeletal muscles at low ionic strength where the protein is in the gel state as it is in muscle. The binding of a divalent cation (Mg2+ or Ca2+) nucleotide complex exposes thiol-1 as well as thiol-2 groups. The long-lived ATPase intermediate occurring at temperatures above 10 degrees C adopts the same conformation with Mg2+ and Ca2+ ions. This intermediate does not protect the thiol-1 and thiol-2 groups but exposes a number of thiol-3 groups which seem to be located distant from the active site. The conformation of the intermediate prevailing in the presence of ATP changes with lowering temperature below 10 degrees C and is identical with that found in the presence of ADP at 0 degree C indicating a change in the rate-limiting step of the hydrolytic cycle. In the absence of divalent cations no such temperature-dependent change in conformation was observed. Evaluation of the activation entropies shows that the structure of the long-lived intermediate occurring above 10 degrees C in the presence of Mg2+ ions goes through a transformation from low to high order at around 20 degrees C. In the case of the monovalent-cation-stimulated ATPase a constant activation energy of around 70 kJ/mol, typical of many enzyme reactions, was found over the entire temperature range from 0--35 degrees C.

Adenosine Diphosphate↗