Amino-acid sequence of parvalbumin from rabbit skeletal muscle.

Enfield, David L.; Ericsson, Lowell H.; Blum, Hubert E.; Fischer, Edmond H.; Neurath, Hans

doi:10.1073/pnas.72.4.1309

Cited by 45 publications

(6 citation statements)

References 26 publications

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“…'Mac Manus & Whitfield (1983). 'Enfield et al (1975). figure 3: Typical plots of In y versus r2 plot for SMCaBP-11.…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a novel molecular weight 11000 calcium-binding protein from smooth muscle

Mani¹,

Kay²

1990

Biochemistry

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A new low molecular weight calcium-binding protein, designated as SMCaBP-11, has been isolated from chicken gizzard using a phenyl-Sepharose affinity column followed by ion-exchange and gel filtration chromatographies. The isolated protein was homogeneous by the criteria of gel electrophoresis in the absence and presence of sodium dodecyl sulfate (NaDodSO4). Molecular weight studies by both sedimentation equilibrium in 6 M guanidine hydrochloride and 15% polyacrylamide-SDS gels indicated the subunit molecular weight to be 11,000, and since a molecular weight of 21,000 was obtained in native solvents, the protein exists as a dimer in benign medium. The amino acid composition of this protein is similar but distinct from other known low molecular weight Ca2(+)-binding proteins. Ca2(+)-binding assays using Arsenazo III (Sigma) indicated the protein to bind 2 mol of Ca2+/subunit. In non-SDS gels, the protein moved faster in the presence of EDTA, suggesting that Ca2+ binding affects its mobility in a manner similar to other smooth muscle calcium-binding proteins such as calmodulin and 67-kDa calcimedin. Upon binding calcium, the protein underwent a conformational change as revealed by UV difference spectroscopy and circular dichroism studies in the aromatic and far-ultraviolet range. When the protein was excited at 280 nm, the tyrosine fluorescence emission maximum was centered at 306 nm. Ca2+ addition resulted in a nearly 15% decrease in intrinsic fluorescence intensity. Fluorescence titration with Ca2+ exhibited two classes of calcium-binding sites with Kd values of 0.2 and 80 microM, in agreement with UV difference spectral data.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…'Mac Manus & Whitfield (1983). 'Enfield et al (1975). figure 3: Typical plots of In y versus r2 plot for SMCaBP-11.…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a novel molecular weight 11000 calcium-binding protein from smooth muscle

Mani¹,

Kay²

1990

Biochemistry

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“…1 b). Out of 110 amino acid residues, 8 are exchanged between mouse and rat, 18 between mouse and rabbit (Enfield et al 1975) and 16 between rat and rabbit. Five residues are identical in rat and rabbit, but differ in mouse PV.…”

Section: (I) Isolation and Sequencing Of A Mouse Parvalbumin Cdna Clonementioning

confidence: 99%

cDNA sequence and chromosomal localization of the mouse parvalbumin gene,Pva

et al. 1989

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In the homozygous condition, the mutation adr (arrested development of righting response) of the mouse causes a myotonia and a drastic reduction of the Ca 2+ -binding protein parvalbumin (PV) in fast muscles. Using a rat PV probe, a mouse cDNA clone was isolated from a Agtll wild-type fast-muscle library and its nucleotide sequence was determined. The protein coding and the 3' nontranslated regions of the mouse gene show extensive homology with the rat PV gene. The result of Southern blot hybridization is consistent with a single copy gene for parvalbumin. Restriction fragment length polymorphisms (RFLPs) between Mus musculus domesticus (e.g. C57BL/6) and Mus spretus (SPE) were detected with the enzymes Eco RI, Pst I, and Sst I. The restriction fragment patterns of DNA samples from 65 individual offspring of (C57BL/6 x SPE)F1 x C57BL/6 backcrosses were tested with the PV probe and matched, for linkage detection, to pre-existing patterns established with various RFLP probes on the same samples. A co-distribution of PVRFLPs with Pvt-1 and Mlvi-2, which had been localized on chromosome 15, was detected. Thus, the structural gene for PV, designated Pva, maps to chromosome 15 of the mouse whereas the adr mutation shows no linkage with markers on this chromosome. Gene locus homology between chromsome 15 of the mouse and chromosome 22 of man (which carries the human PV gene) is discussed.

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“…Positions whose amino acid is identical in all 20 sequences are enclosed in boxes. The taxa are: pike = Esox lucinus (Frankenne et al 1973;Gerday 1976); coelacanth = Latimeria chalumnae (Jauregui-Adell and Pechire 1978; Pechere et al 1978); amphiuma = Amphiuma means; frog = Rana esculentu (Capony et al 1975;Jauregui-Adell et al 1982); rabbit = Oryctolugus cuniculus (Enfield et al 1975); thomback ray = Ruju cluveutu (Thatcher and Pechere 1977); turtle = Gruptemys geogruphicu; boa = Boa constrictor; whiting = Gudus merlungus (Joassin and Gerday 1977); cod = Gudus cullarias (Elsayed and Bennich 1975); hake = Merluccius merluccius ); chub = Leuciscus cephulus (Gerday et al 1978); electric eel = Electrophorus electricus (Zhu et al 1984 bridge, and Leu-79, which is responsible for hydrogen binding with . The function of Phe-72 and Thr-84 is not known.…”

Section: Discussionmentioning

confidence: 99%

“…The recent studies on the parvalbumins in muscles of rabbit (Lehky et al 1974;Enfield et al 1975), rat (Berchtold et al 1982), and chicken (Heizmann and Strehler 1979), however, have revealed the presence of this protein in a wider range of vertebrates. Because of their relative ease of purification and small size, interest in this family of homologous proteins in systematic study has increased (Pechire et al 1973;Goodman and Pechere 1977;Goodman et al 1979).…”

Section: Introductionmentioning

confidence: 99%

Amino acid sequences of lower vertebrate parvalbumins and their evolution: parvalbumins of boa, turtle, and salamander.

Maeda

Zhu²,

Fitch³

1984

Molecular Biology and Evolution

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One major parvalbumin each was isolated from the skeletal muscle of two reptiles, a boa snake, Boa constrictor, and a map turtle, Graptemys geographica, while two parvalbumins were isolated from an amphibian, the salamander Amphiuma means. The amino acid sequences of all four parvalbumins were determined from the sequences of their tryptic peptides, which were ordered partially by homology to other parvalbumins. Phylogenetic study of these and 16 other parvalbumin sequences revealed that the turtle parvalbumin belongs to p lineage, while the salamander sequences belong, one each, to the a and p lineages defined by Goodman and Pechire ( 1977). Boa parvalbumin, however, while belonging to the p lineage, clusters within the fish in all reasonably parsimonious trees. The most parsimonious trees show many parallel or back mutations in the evolution of many parvalbumin residues, although the residues responsible for Ca*+ binding are very well conserved. These most parsimonious trees show an actinopterygian rather than a crossoptyrigian origin of the tetrapods in both the u and p groups. One of two electric eel parvalbumins is evolving more than 10 times faster than its paralogous partner, suggesting it may be on its way to becoming a pseudogene. It is concluded that varying rates of amino acid replacement, much homoplasy, considerable gene duplication, plus complicated lineages make the set of parvalbumin sequences unsuitable for systematic study of the origin of the tetrapods and other higher-taxa divergence, although it may be suitable within a genus or family.

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Amino-acid sequence of parvalbumin from rabbit skeletal muscle.

Cited by 45 publications

References 26 publications

Isolation and characterization of a novel molecular weight 11000 calcium-binding protein from smooth muscle

Isolation and characterization of a novel molecular weight 11000 calcium-binding protein from smooth muscle

cDNA sequence and chromosomal localization of the mouse parvalbumin gene,Pva

Amino acid sequences of lower vertebrate parvalbumins and their evolution: parvalbumins of boa, turtle, and salamander.

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