Über die Sedimentationskonstante von Muskelproteinen.

Deuticke, H. J.

doi:10.1515/bchm2.1934.224.5-6.216

Cited by 40 publications

(4 citation statements)

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“…Their properties include acidic isoelectric points, amino acid compositions rich in phenylalanine and alanine, and binding sites for 2 mol of calcium/mol of protein with dissociation constants of 10"7-1CT9 M [reviewed in Kretsinger (1980)]. Calciumbinding parvalbumin was first identified in frog muscle by Deuticke (1934) and further characterized by Hamoir (1951).…”

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confidence: 99%

Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Kumar¹,

Lee²,

Edwards³

1990

Biochemistry

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The crystal structure of carp parvalbumin (pI = 4.25) has been refined by restrained least-squares analysis employing X-ray diffractometer data to 1.5-A resolution. The final residual for 12,653 reflections between 10 and 1.5 A with I(hkl) greater than 2 sigma(I) is 0.215. A total of 74 solvent molecules were included in the least-squares analysis. The root mean square deviation from ideality of bond lengths is 0.024 A. The model has a root mean square difference of 0.59 A from the positions of the main-chain atoms in a previously reported structure [Moews, P. C., & Kretsinger, R. H. (1975) J. Mol. Biol. 91, 201-228], which was refined by difference Fourier syntheses using data collected by film to 1.9 A. Although the overall features of the two models are very similar, there are significant differences in the amino-terminal region, which was extensively refit, and in the number of oxygen atoms liganding calcium in the CD and EF sites, which increased from six to seven in the CD site and decreased from eight to seven in the EF site.

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confidence: 99%

Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Kumar¹,

Lee²,

Edwards³

1990

Biochemistry

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“…The radiation-responsive PV-α detected in this study is primarily an intracellular Ca 2+ -binding protein with varied functional roles. Identified initially in Amphibian and Piscean muscle cells [44] , it is part of an important family of proteins involved in regulating Ca 2+ switching inside the cells [ 45 , 35 ]. While its prevalence in cardiomyocytes, neurons and few other cell types has been well established [ 46 , 34 ], there is no reported evidence of its presence in erythrocytes till date.…”

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Identification of radiation responsive RBC membrane associated proteins (RMAPs) in whole-body γ-irradiated New Zealand white rabbits

Purkayastha

Grover

Mukherjee

et al. 2023

Biotechnology Reports

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“…Parvalbumins were first found in tissues where they are abundant, namely in the muscles of ectotherm vertebrate species like frogs [ 12 ] and fish [ 13 , 14 ]. Already early on, it was clear that single species can have multiple different forms of these molecules, and the family name “parvalbumins” was chosen because of their small size ( parvus is Latin for small) and their solubility in water akin to albumin [ 14 ].…”

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Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species

Dijkstra

Kondo

2022

Biology

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Parvalbumins are small molecules with important functions in Ca2+ signaling, but their sequence comparisons to date, especially in fish, have been relatively poor. We here, characterize sequence motifs that distinguish parvalbumin subfamilies across vertebrate species, as well as those that distinguish individual parvalbumins (orthologues) in fish, and map them to known parvalbumin structures. As already observed by others, all classes of jawed vertebrates possess parvalbumins of both the a-parvalbumin and oncomodulin subfamilies. However, we could not find convincing phylogenetic support for the common habit of classifying all non-a-parvalbumins together as “b-parvalbumins.” In teleost (modern bony) fish, we here distinguish parvalbumins 1-to-10, of which the gene copy number can differ between species. The genes for a-parvalbumins (pvalb6 and pvalb7) and oncomodulins (pvalb8 and pvalb9) are well conserved between teleost species, but considerable variation is observed in their copy numbers of the non-a/non-oncomodulin genes pvalb1-to-5 and pvalb10. Teleost parvalbumins 1-to-4 are hardly distinguishable from each other and are highly expressed in muscle, and described allergens belong to this subfamily. However, in some fish species a-parvalbumin expression is also high in muscle. Pvalb5 and pvalb10 molecules form distinct lineages, the latter even predating the origin of teleosts, but have been lost in some teleost species. The present study aspires to be a frame of reference for future studies trying to compare different parvalbumins.

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Über die Sedimentationskonstante von Muskelproteinen.

Cited by 40 publications

References 0 publications

Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Identification of radiation responsive RBC membrane associated proteins (RMAPs) in whole-body γ-irradiated New Zealand white rabbits

Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species

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