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639


THE SIGNIFICANCE OF NEW IMAGING TECHNIQUES IN STUDIES OF BRAIN METABOLISM

LAJTHA A; BATTISTIN L
BIOSIS:PREV198732056644
ISSN: 0736-4563
CID: 115566

DOES CHRONIC NICOTINE ALTER NEUROTRANSMITTER RECEPTORS INVOLVED IN PARKINSONS-DISEASE [Meeting Abstract]

REILLY, MA; LAPIN, EP; LAJTHA, A; MAKER, HS
ISI:A1986A294900408
ISSN: 0014-9446
CID: 115567

DOES TRITIATED TETRACAINE BINDING TO SYNAPTOSOMES REPRESENT SODIUM CHANNELS [Meeting Abstract]

REITH M E A; KIM S S; LAJTHA A
BIOSIS:PREV198631105561
ISSN: 0190-5295
CID: 115568

EFFECT OF ASCORBIC-ACID ON THE SYNAPTOSOMAL UPTAKE OF TRITIATED 1 METHYL-4-PHENYLPYRIDINIUM ION TRITIATED DOPAMINE AND TRITIATED GAMMA AMINOBUTYRIC-ACID [Meeting Abstract]

SERSHEN H; DEBLER E A; LAJTHA A
BIOSIS:PREV198732008050
ISSN: 0190-5295
CID: 115569

REGIONAL DIFFERENCES IN THE EFFECT OF METHYLPHENYL-6-TETRAHYDROPYRIDINE ON TYROSINE HYDROXYLASE ACTIVITY IN MICE [Meeting Abstract]

SZIRAKI I; JUHASZ M; KOBOR G; LAJTHA A; VADASZ C
BIOSIS:PREV198631115084
ISSN: 0190-5295
CID: 115570

EFFECT OF GLYCINE DERIVATIVES ON BEHAVIORAL-CHANGES INDUCED BY 3-MERCAPTOPROPIONIC ACID OR PHENCYCLIDINE IN MICE

TOTH, E; WEISS, B; BANAYSCHWARTZ, M; LAJTHA, A
ISI:A1986D425000001
ISSN: 0362-2428
CID: 115571

ETHOLOGICAL ANALYSIS OF OPEN-FIELD BEHAVIOR IN HIGHLY INBRED MOUSE STRAINS, THEIR F1 HYBRIDS, AND REPLICATED F2 GENERATIONS [Meeting Abstract]

VADASZ, C; KOBOR, G; LAJTHA, A
ISI:A1986F526400077
ISSN: 0001-8244
CID: 115572

HEREDITARY EFFECTS ON MESOTELENCEPHALIC TYROSINE HYDROXYLASE ACTIVITY AND COMPONENTS OF OPEN-FIELD BEHAVIOR [Meeting Abstract]

VADASZ C; KOBOR G; SZIRAKI I; LAJTHA A
BIOSIS:PREV198732016756
ISSN: 0190-5295
CID: 115573

GENETICS OF MESENCEPHALIC TYROSINE HYDROXYLASE ACTIVITY

VADASZ C; SZIRAKI I; MURTHY L R; VADASZ I K; BADALAMENTI A F; KOBOR G; LAJTHA A
BIOSIS:PREV198631116078
ISSN: 0167-6253
CID: 115574

An opiate receptor-associated aminopeptidase that degrades enkephalins

Hui KS; Gioannini T; Hui M; Simon EJ; Lajtha A
During the purification of opiate receptor by affinity chromatography on wheat germ agglutinin-agarose, an aminopeptidase is coeluted with the receptor. Virtually all of both the enzyme and the receptor is retained on the hydroxylapatite column. The aminopeptidase functions optimally at neutral pH and is activated by Mn2+. The enzyme is sensitive to dithiothreitol, is inhibited by amastatin and bestatin, and is insensitive to puromycin. The enzyme seems to be linked to the receptor, since its activity is enhanced by D-Ala2-Met-enkephalinamide or naltrexone. The properties of this aminopeptidase indicate that it is distinct from neutral arylamidase, leucine-aminopeptidase, aminopeptidases A and B, brain acidic aminopeptidase, and the membrane aminoenkephalinase that we purified recently (4)
PMID: 2997642
ISSN: 0364-3190
CID: 60406