Results 161 to 170 of about 10,107 (221)

Comparison between eDNA and traditional morphological methods for fish diversity monitoring in rivers. [PDF]

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Yu Y, Shao M, Zhou H, Su F, Guan P, Ding L, Ma T, Zhou B, Xu S, Song S, Qu B.   +10 more
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Hexokinase III from Rana catesbeiana

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1978
1. Hexokinase III was partially purified from the liver of the American bullfrong, Rana catesbeiana, using DEAE-cellulose column chromatography. 2. It was inhibited by glucose concentrations above 5 x 10(-5) M (pH 5.9), 10(-4) M (pH 6.7) or 10(-3) M (pH 7.5). 3. There was virtually no inhibition by excess glucose at pH 8.7. 4.
D, Balinsky, H J, Fromm
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Oxygen uptake in bullfrog tadpoles (Rana catesbeiana)

The Journal of Experimental Zoology, 1998
Weight-specific rates of aquatic oxygen consumption (VO2, microliter O2 g-1 h-1) at 23 degrees C were determined for water-breathing (e.g., forcibly submerged) bullfrog tadpoles as functions of stage of development and O2 tension (PO2). The VO2 at an O2 tension near that of air-saturated water (PO2 approximately 154 mmHg) was independent of stage of ...
W C, Crowder, M, Nie, G R, Ultsch
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Microbiological Studies on Septicemic Bullfrogs (Rana catesbeiana)

American Journal of Veterinary Research, 1974
SUMMARY Microbiological studies were made on Louisiana bullfrogs and tadpoles (Rana catesbeiana) with signs of classic red-leg disease. A group of bacteria commonly found in the aquatic environment was isolated from the blood of the diseased frogs. The same isolates induced red-leg disease when inoculated into healthy frogs and tadpoles.
J C, Glorioso, R L, Amborski, G F, Amborski, D D, Culley   +3 more
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Immunoglobulins in the Developing Amphibian, Rana Catesbeiana

The Journal of Immunology, 1973
Abstract Rana catesbeiana tadpoles contain high molecular weight and low molecular weight immunoglobulins that closely resemble, in structural and antigenic features, the corresponding immunoglobulins in adult bullfrogs. Although the low molecular weight immunoglobulins are antigenically heterogeneous, all the antigenic species found in ...
C L, Geczy, P C, Green, L A, Steiner
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Neurohypophysial function in bullfrog (Rana catesbeiana) tadpoles

General and Comparative Endocrinology, 1970
Abstract Bullfrog tadpoles retain water when injected with vasotocin. This response is very small in young tadpoles but increases later, especially just prior to metamorphorsis. Vasotocin also increases the osmotic permeability of the skin in such tadpoles.
P J, Bentley, L, Greenwald
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Physiological color change in the bullfrog,Rana catesbeiana

Journal of Experimental Zoology, 1999
Adults of Rana catesbeiana maintained for 4 days in 12:12 light/dark regimen exhibited a rhythmic color change of 24 hr. Under constant light, however, the rhythm disappeared, and the reflectance values gradually became greater, that is the animals became lighter.
C R, Camargo, M A, Visconti, A M, Castrucci   +2 more
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Low Molecular Weight Immunoglobulins in Rana Catesbeiana Tadpoles

The Journal of Immunology, 1976
Abstract Rana catesbeiana tadpoles formed high and low m. w. antibodies in response to immunization with a bacteriophage. Although the neutralizing activity associated with the low m. w. immunoglobulins was relatively weak, the existence of antibodies in this class was clearly demonstrated by radioimmunoelectrophoresis.
C, Green, L A, Steiner
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Pharmacokinetics of kanamycin in the bullfrog, Rana catesbeiana

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1987
1. Kanamycin disposition was studied in bullfrogs (Rana catesbeiana) following single doses IP. Both plasma t1/2 and Vd of the drug increased with increasing time after drug indicating redistribution and tight binding of kanamycin to deep tissue compartments. 2. Kanamycin was eliminated unchanged with a t1/2 plasma = 27 hr; perilymph = 89 hr; endolymph
K E, Fox, N J, Russell
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Catalytic lectin (leczyme) from bullfrog (Rana catesbeiana) eggs

International Journal of Oncology, 1996
Catalytic lectins (leczymes) of frog eggs are sialic acid-binding lectins that have intrinsic RNase activity. They inhibit tumor cell proliferation in vitro and in vivo, although their cytotoxic mechanism remains unclear. RNase A has no tumoricidal activity.
K, Nitta, K, Ozaki, Y, Tsukamoto, M, Hosono, Y, Ogawakonno, H, Kawauchi, Y, Takayanagi, S, Tsuiki, S, Hakomori   +8 more
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