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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomedical science 3 (1996), S. 203-210 
    ISSN: 1423-0127
    Keywords: Ile7-angiotensin III ; Bestatin ; Osmotic minipump ; Drinking response ; Spontaneously hypertensive rats ; Normotensive rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We examined the physiologic role of endogenous brain angiotensin III (AIII), an active degradative product of angiotensin II, in drinking behavior. Adult, male spontaneously hypertensive (SH) and Wistar-Kyoto normotensive (WKY) rats that were instrumented with an intracerebroventricular (i.c.v.) cannula connected to an osmotic minipump for chronic infusion were used. 7-day i.c.v. infusion of the specific AIII antagonist, Ile7-AIII (10 or 100 pmol/min), resulted in no significant alteration in daily (24 h), diurnal (8:00 a.m.-8:00 p.m.) or nocturnal (8:00 p.m.-8:00 a.m.) basal water intake in both SH and WKY rats. Similar results were obtained with i.c.v. infusion of the aminopeptidase inhibitor, bestatin (150 or 300 pmol/min), given alone or simultaneously with Ile7-AIII (10 pmol/min). Rats that were water-deprived for the first 3 days of 7-day infusion of Ile7-AIII consumed significantly less water during the first 2 h after water became available. Furthermore, the accumulated water intake during the first 24 h was appreciably greater in SH than WKY rats. We interpret these results to suggest that the endogenous brain AIII may not be tonically involved in fluid homeostasis. Instead, it must be activated under conditions of dehydration, such as water deprivation, particularly in the SHRs, to initiate drinking behavior.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4943
    Keywords: Snake venom ; presynaptic neurotoxin ; β1-bungarotoxin ; A chain and B chain of β1-bungarotoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interchain disulfide bond between A chain and B chain of β1-bungarotoxin (β1-Bgt) was selectively cleaved by dithiothreitol, and the A and B chains were separated by HPLC. The separated A and B chains did not show detectable enzymatic activity and lethal toxicity, but exhibited an immunoreactivity with anti-β1-Bgt antibody. Analytical isoelectrofocusing revealed that the A chain is a neutral subunit with pI=7.4, and the B chain is a basic one with pI=9.6. The A chain exhibited a Ca2+-binding ability as revealed by fluorescence measurement. Moreover, fluorescence studies showed that the intact interchain disulfide bond is essential for maintaining the hydrophobic character of substrate binding site in β1-Bgt and stabilizing the architectural environment of Trp-19 in the A chain. However, combination of the A chain and B chain failed to restore the biological activities and physicochemical properties which the intact β1-Bgt possessed. These, together with our previous result that the Trp-19 of the A chain is involved in substrate binding, suggest that the integrity of the interchain disulfide bond favors the maintenance of the active conformation of β1-Bgt.
    Type of Medium: Electronic Resource
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