Searched for: in-biosketch:yes
person:lajtha01
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