Kinetic characterization of the lactate dehydrogenase (LDH-B4) allozymes of Fundulus heteroclitus.
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چکیده
منابع مشابه
The Adaptive Cline at LDH (Lactate Dehydrogenase) in Killifish Fundulus heteroclitus Remains Stationary After 40 Years of Warming Estuaries.
Since the 1970s, water temperatures along the Atlantic seaboard of the United States have risen by an average of 0.5 °C in summer months and 2.2 °C in winter months. In response, the distribution and abundance of several nearshore species have changed dramatically, but no study has attempted to document whether estuarine populations have evolved greater thermal tolerance. Here, we re-examine th...
متن کاملMolecular basis of evolutionary adaptation at the lactate dehydrogenase-B locus in the fish Fundulus heteroclitus.
At the extremes of its natural distribution, populations of the common killifish Fundulus heteroclitus experience a difference of more than 15 degrees C in mean annual temperature. These populations are virtually fixed for two different codominant alleles at the heart-type lactate dehydrogenase locus (Ldh-B) which code for allozymes with different and adaptive kinetic responses to temperature. ...
متن کاملLactate dehydrogenase-B cDNA from the teleost Fundulus heteroclitus: evolutionary implications.
A cDNA that encodes the heart-type lactate dehydrogenase (LDH-B) from the teleost fish Fundulus heteroclitus was cloned and sequenced. The protein encoded by the cDNA was analyzed in relation to 13 LDH proteins from a variety of taxa. One of the deductions from this analysis is that LDH-B proteins have residues in the active site that are unique and that may be important in determining the bioc...
متن کاملGenetic organization and adaptive response of allozymes to ecological variables in Fundulus heteroclitus.
Populations of Fundulus heteroclitus, (Cyprinodontidae) a widespread coastal marine fish, were studied in control and artificially heated environments on the North Shore of Long Island, New York to determine (1) patterns of variation in biochemical phenotypes and (2) the extent to which this variation reflected adaptation to environmental characteristics. Variation at three of twelve polymorphi...
متن کاملA further study of human seminal plasma lactate dehydrogenase-C4 (LDH-C4): kinetic properties of LDH-C4.
Lactate dehydrogenase-C4 (LDH-C4) from human seminal plasma was purified by 40-60% (NH4)2SO4 precipitation, Oxamate-Sepharose 4B affinity column chromatography and AMP affinity column chromatography. Enzyme kinetic studies of human seminal plasma LDH-C4 were performed with purified LDH -C4. The human LDH-C4 exhibits a much higher affinity for pyruvate and alpha-ketovalerate than lactate. Appare...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43604-0