A dynamic theory of thin layer chromatography

Belenky, B.G.; Нестеров, В. В.; Gankina, E.S.; Smirnov, M. M.

doi:10.1016/s0021-9673(01)86084-2

Cited by 24 publications

(5 citation statements)

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“…Thus, the amino acid composition, molecular mass, N terminal amino acid (alanine), and polarity index (45% [26]) of the protein isolated from the "warm" vari ant of Y. enterocolitica were similar to those of porins of other gram negative bacteria [5,6,9,15,18], and this allows us to relate the protein under study to this class of integral membrane proteins.…”

Section: Resultsmentioning

confidence: 89%

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OmpC-like porin from outer membrane of Yersinia enterocolitica: Molecular structure and functional activity

Vostrikova

Isaeva

Likhatskaya

et al. 2013

Biochemistry Moscow

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OmpC-like porin was isolated from the outer membrane (OM) of Yersinia enterocolitica cultured at 37°C (the "warm" variant) and its physicochemical and functional properties were studied. The amino acid sequence of OmpC porin was established, and the primary structure and transmembrane topology of this protein were analyzed in comparison with the OmpF porin isolated from Y. enterocolitica cultured at 6°C (the "cold" variant). Both porins of Y. enterocolitica had a high homology degree (65%) between themselves and with OmpC and OmpF porins from OM of Escherichia coli (58 and 76% homology, respectively). The secondary structure of OmpC and OmpF porins from OM of Y. enterocolitica consists of 16 β-strands connected by short "periplasmic" and longer "extracellular" loops with disordered structure, according to the topological model developed for porins of E. coli. The molecular structures of OmpC and OmpF porins of Y. enterocolitica have significant differences in the structure of the "extracellular" loops and in the position of one of three tryptophan residues. Using the bilayer lipid membrane (BLM) technique, pores formed by OmpC porin of Y. enterocolitica were shown to differ in electrophysiological characteristics from channels of OmpF protein of this microorganism. The isolated OmpC porin reconstructed into BLM displayed functional plasticity similarly to OmpF protein and nonspecific porins of other enterobacteria. The conductivity level of the channels formed by this protein in the BLM was regulated by value of the applied potential.

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Section: Resultsmentioning

confidence: 89%

“…Dansyl derivatives of amino acids were identified by two dimensional thin layer chromatog raphy on plates (5 × 5 cm) with a bound silica gel layer [26].…”

Section: Methodsmentioning

confidence: 99%

OmpC-like porin from outer membrane of Yersinia enterocolitica: Molecular structure and functional activity

Vostrikova

Isaeva

Likhatskaya

et al. 2013

Biochemistry Moscow

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“…Upon the further assumptions of Belenky's dynamic model (1,2), the following dependence was established, defining concentration of solute at time t and at a given point of the sorbent layer, described by the coordinates x and y (see 2D L R f t > 2 T) Rft \ (3) where q is the total amount of solute in a chromatographic spot; R f is the basic TLC parameter introduced in Section III.C; D L denotes the effective diffusion coefficient that characterizes broadening of a chromatographic spot; v is the migration velocity of the chromatographic spot center; and T is the parameter representing a time lag in establishing equilibrium between the mobile and stationary phases (r is also a function of the particle size of a solid bed). From the main dependence of Belenky's model it follows that the concentration of solute in the chromatographic spot is described by a two-dimensional Gaussian distribution function, which can be rewritten in a simpler form: (4) where (5) Mierzejewski's approach (3) to the problem was different.…”

Section: B Broadening Of Chromatographic Spotsmentioning

confidence: 99%

Theory and Mechanism of Thin-Layer Chromatography

Kaczmarski¹,

Kowalska²,

Prus³

2003

Handbook of Thin-Layer Chromatography

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“…Identity, purity and homogeneity of proteins were tested by two-dimensional gel electrophoresis in urea [16], one-dimensional gel electrophoresis in sodium dodecylsulfate [17], N-terminal amino acid determination [18] and amino acid analysis. The purity of the preparations was more than 90 x.…”

Section: Yield Of Proteins and Purity Testsmentioning

confidence: 99%

Optical Characteristics of All Individual Proteins from the Small Subunit of Escherichia coli Ribosomes

Venyaminov¹,

Gogia²

1982

European Journal of Biochemistry

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The procedure of isolation and renaturation of all ribosomal proteins from the 30-S subunit of Escherichia coli ribosomes is described. Absorption spectra of these proteins in the near-ultraviolet region have been measured and molar absorption coefficients have been determined on the basis of nitrogen content. Molar absorption coefficients have been calculated for 20 proteins with a known amino acid sequence and the calculated values have been compared with the experimentally determined ones. The absorption spectra obtained allow an easy, precise and highly reproducible spectrophotometric determination of the concentration of individual ribosomal proteins.Circular dichroic spectra of 21 individual proteins from the 30-S subunit of E. coli ribosomes were measured in the range 284-310 nm. The secondary structure of the proteins studied was calculated from the spectra in the range 190-240 nm. Almost all proteins (except proteins S12, S17, S18 and S19) are characterized by a high content of secondary structure. Circular dichroic spectra in the near-ultraviolet region (240 -310 nm) indicate that the side groups of aromatic amino acids are fixed in the tertiary structure of the proteins studied.Some internal characteristics (independent of the measurement conditions) of the circular dichroic spectrum in the far-ultraviolet region were proposed as a measure of the resemblance to the native state of ribosomal proteins ; these characteristics may be useful for comparison of protein preparations obtained by different methods in different laboratories. Ribosomal proteins, as a rule, have no actually known physiological functions in the isolated state. Therefore the concept of the native origin of these proteins can be defined only by the identity of their structure and properties in the isolated state to those within the ribosome. The assembly of active ribosomal subunits from the individual isolated proteins cannot prove their native existence as proteins are used in excess during the assembly; they can renature in the process of assembly and the number of active subunits formed is not Therefore from general considerations it is possible to assume that a smaller radius of gyration [6], a more folded tertiary structure (according to NMR data) [7 -91, a higher cooperativity at heat denaturation [9] and a larger content of ordered secondary structure (secondary folding) [I 01 indicate a greater structural identity to the native state of ribosomal proteins.In the study reported here, circular dichroic (CD) spectra of all individual proteins from the small subunit of Escherichia Abbreviations. RNP, ribonucleoprotein; CD, circular dichroism 100 %.coli ribosomes isolated by LiCl/urea extraction and then transferred to non-denaturing conditions were measured in the range 184-310 nm. Of course, we cannot be absolutely certain that for all the proteins isolated under denaturing conditions, a complete renaturation was achieved ; however, we consider that the CD spectra presented are optical characteristics of the individual ribosom...

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A dynamic theory of thin layer chromatography

Cited by 24 publications

References 0 publications

OmpC-like porin from outer membrane of Yersinia enterocolitica: Molecular structure and functional activity

OmpC-like porin from outer membrane of Yersinia enterocolitica: Molecular structure and functional activity

Theory and Mechanism of Thin-Layer Chromatography

Optical Characteristics of All Individual Proteins from the Small Subunit of Escherichia coli Ribosomes

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