Morph-Specific Proteins in Pollen and Styles of Distylous Turnera (Turneraceae)

Genetics ◽  
1997 ◽  
Vol 146 (2) ◽  
pp. 669-679
Author(s):  
Andreas Athanasiou ◽  
Joel S Shore
Keyword(s):  
Isoelectric Focusing ◽  
Isozyme Markers ◽  
Unlinked Locus ◽  
Full Expression ◽  
Isoelectric Points ◽  
Isozyme Loci ◽  
Specific Proteins ◽  
S Allele

We used nondenaturing isoelectric focusing (IEF) in a survey of plants from 11 populations to identify style and pollen proteins unique to the short-styled morph of Turnera scabra, T. subulata and T. krapovickasii. Three protein bands [approximately isoelectric points (pIs) 6.1, 6.3 and 6.5] were found only in styles and stigmas of short-styled plants while two bands (approximately pIs 6.7 and 6.8, M  r 56 and 59 kD) occur only in pollen of short-styled plants. Some of these bands appear very late in development, within 24 hr before flowering. Two isozyme loci were mapped to an 8.7 cM region spanning the distyly locus. Using these isozyme markers we identified progeny exhibiting recombination adjacent to the distyly locus. No recombinants between the distyly locus and the locus or loci controlling the presence of the short-styled morph-specific proteins were obtained. This suggests that the loci encoding these proteins are either extremely tightly linked to the distyly locus and in complete disequilibrium with the S allele or exhibit morph-limited expression. Crosses to a plant showing an unusual style protein phenotype demonstrated that an additional unlinked locus is required for full expression of the style proteins. The function of the morph-specific proteins is unknown

Isoelectric focusing of insulin, 125I-insulin and the 125I-insulin-antibody complex

1979 ◽  
Vol 44 (6) ◽  
pp. 1828-1834
Author(s):  
Asja Šiševa ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Stephan P. Ditzov ◽  
Luben M. Sirakov
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Insulin Antibody ◽  
Isoelectric Points ◽  
Antibody Complex ◽  
And Storage ◽  
Acid Region ◽  
Three Components

Isoelectric focusing on polyacrylamide gel columns of three native crystalline commercial preparations of insulin and 125I-labelled insulin was carried out. All the compounds studied contained three components of different isoelectric points. The largest fraction, having pI 5.60 ± 0.05, was common to all preparations. The other two fractions were situated in the acid region of pH between pI 4.5 and 5.2. The presence of these fractions is explained by the contamination of crystalline insulins by proinsulin and by the formation of des-amido derivatives during the dissolving and storage of insulin samples, and, in case of labelled insulin, also by the presence of heavily iodinated insulin and contaminating components. The isoelectric focusing of the complex 125I-insulin-antibody showed a peak of radioactivity having pI 6.15 ± 0.05.

scholarly journals Isoelectric focusing of glutathione S-transferases from rat liver and kidney

1978 ◽  
Vol 175 (3) ◽  
pp. 937-943 ◽  
Author(s):  
Barbara F. Hales ◽  
Valerie Jaeger ◽  
Allen H. Neims
Keyword(s):  
Substrate Specificity ◽  
Isoelectric Focusing ◽  
Transferase Activity ◽  
Sprague Dawley ◽  
Substrate Specificities ◽  
Liver Cytosol ◽  
Sprague Dawley Rats ◽  
Isoelectric Points ◽  
Liver And Kidney ◽  
Glutathione S Transferases

The glutathione S-transferases that were purified to homogeneity from liver cytosol have overlapping but distinct substrate specificities and different isoelectric points. This report explores the possibility of using preparative electrofocusing to compare the composition of the transferases in liver and kidney cytosol. Hepatic cytosol from adult male Sprague–Dawley rats was resolved by isoelectric focusing on Sephadex columns into five peaks of transferase activity, each with characteristic substrate specificity. The first four peaks of transferase activity (in order of decreasing basicity) are identified as transferases AA, B, A and C respectively, on the basis of substrate specificity, but the fifth peak (pI6.6) does not correspond to a previously described transferase. Isoelectric focusing of renal cytosol resolves only three major peaks of transferase activity, each with narrow substrate specificity. In the kidney, peak 1 (pI9.0) has most of the activity toward 1-chloro-2,4-dinitrobenzene, peak 2 (pI8.5) toward p-nitrobenzyl chloride, and peak 3 (pI7.0) toward trans-4-phenylbut-3-en-2-one. Renal transferase peak 1 (pI9.0) appears to correspond to transferase B on the basis of pI, substrate specificity and antigenicity. Kidney transferase peaks 2 (pI8.5) and 3 (pI7.0) do not correspond to previously described glutathione S-transferases, although kidney transferase peak 3 is similar to the transferase peak 5 from focused hepatic cytosol. Transferases A and C were not found in kidney cytosol, and transferase AA was detected in only one out of six replicates. Thus it is important to recognize the contribution of individual transferases to total transferase activity in that each transferase may be regulated independently.

scholarly journals GENETICALLY CONTROLLED VARIATION OF "ACID" β-GALACTOSIDASE DETECTED IN Rattus norvegicus BY ISOELECTRIC FOCUSING

Genetics ◽  
1982 ◽  
Vol 100 (3) ◽  
pp. 455-473
Author(s):  
Tommy C Douglas ◽  
Kathryn A Kimmel ◽  
Patti E Dawson
Keyword(s):  
Isoelectric Focusing ◽  
Rattus Norvegicus ◽  
Rat Kidney ◽  
Ph Dependence ◽  
Point Mutations ◽  
Autosomal Locus ◽  
Ph Optimum ◽  
Banding Patterns ◽  
Isoelectric Points ◽  
Significant Linkage

ABSTRACT Two genetically variant forms of rat "acid" β-galactosidase were found to differ in isoelectric point and pH dependence, but not in thermostability or sensitivity to inhibition by p-mercuribenzoate (PMB). The results of two backcrosses and an intercross indicated that the isoelectric focusing phenotypes are controlled by two codominant alleles at a single autosomal locus, for which we propose the name Glb-1. No significant linkage between Glb-1 and albino (LG I), brown (LG II), or hooded (LG VI) was observed. Strain-specific differences in total levels of kidney β-galactosidase were detected, but it is not yet known whether the variation is controlled by genes linked to Glb-1. Experiments in which organ homogenates were incubated with neuraminidase indicated that the genetically variant forms do not result from differences in sialylation, though sialylation does appear to be largely responsible for the presence of multiple bands within each phenotype and for differences in the banding patterns of β-galactosidases derived from different organs. The β-galactosidase present in the bands used for Glb-1 typing resembles human GM1 gangliosidase (GLB1) with respect to pH optimum, substrate specificity, and susceptibility to inhibition by PMB. It also appears that Glb-1 is homologous with the Bgl-e locus of the mouse. In rats as in mice the genetically variant bands of β-galactosidase are active at acid pH and have relatively high isoelectric points. In both species these bands are readily detectable in kidney homogenates, and can be revealed in homogenates of liver or spleen following treatment with neuraminidase. The presence of the same β-galactosidase bands in homogenates of rat kidney and small intestine as well as in neuraminidase-treated homogenates of liver and spleen suggests that the Glb-1 variants differ by one or more point mutations in the structural gene for "acid" β-galactosidase.

Shifts of isoelectric points between cellular and secreted antibodies as revealed by isoelectric focusing and immobilized pH gradients

1990 ◽  
Vol 11 (11) ◽  
pp. 966-969 ◽  
Author(s):  
Elisabeth Wenisch ◽  
Susanne Reiter ◽  
Susanne Hinger ◽  
Franz Steindl ◽  
Christa Tauer ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Ph Gradients ◽  
Isoelectric Points

Isolation and Identification of Poplar Isoplastocyanins

2010 ◽  
Vol 65 (3-4) ◽  
pp. 225-230 ◽  
Author(s):  
Mitko I. Dimitrov ◽  
Anthony A. Donchev ◽  
Alexandra C. Shosheva ◽  
Vladimir I. Getov ◽  
Nedyalka P. Terezova ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Physiological Significance ◽  
Purification Procedure ◽  
Isolation And Identification ◽  
Isolation And Purification ◽  
The Third ◽  
Present Procedure ◽  
Vis Spectroscopy ◽  
Isoelectric Points

An improved four-stage isolation and purification procedure for preparing poplar isoplastocyanins is described in detail. Absorbance (UV-VIS) spectroscopy and isoelectric focusing (IEF) are used to determine the protein purity and identity. The present procedure increases twice the total plastocyanin (PC) yield. Four PC isoform fractions are consecutively isolated at the third chromatographic step: oxidized PCa(II) and PCb(II) and reduced PCb(I) and PCa(I). PCa(II) and PCb(II) obtained at the fourth chromatographic step are highly purified PC isoforms which show the purity index (p.i.) A278/A597 ≤ 0.85. Isoelectric points (pI values) of the PC isoforms are found to be at pH 3.92 ± 0.04 for PCa and at pH 3.85 ± 0.02 for PCb. The results of appropriate biological experiments that include the highly purified poplar PC isoforms could give answers to the questions about the physiological significance of PC dimorphism for photosynthesis.

Relation of age to isoenzyme pattern and total activity of amylase in serum.

1981 ◽  
Vol 27 (3) ◽  
pp. 451-454 ◽  
Author(s):  
P J Bossuyt ◽  
R Van den Bogaert ◽  
S L Scharpé ◽  
Y Van Maercke
Keyword(s):  
Thin Layer ◽  
Isoelectric Focusing ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Total Activity ◽  
Ph Gradient ◽  
Isoenzyme Pattern ◽  
Isoelectric Points ◽  
Age Dependent ◽  
Gel Isoelectric Focusing

Abstract Pancreatic and salivary isoenzymes of amylase were determined in serum from 70 subjects. Thin-layer gel/isoelectric focusing was used to separate the isoenzymes. Because other studies (J. Lab. Clin. Med. 90: 141-151, 1977) show that the major isoamylases have isoelectric points between 5.8 and 7.2, we focused the sera on polyacrylamide gel plates with a pH gradient from 5.5 to 8.5. The separated amylase fractions were made visible by direct incubation with a commercially available dye-starch polymer. Isoelectric focusing proved to be convenient, precise, and reproducible, and it can be used as a routine analysis to detect even slight changes in serum amylase distributions. We found that the isoamylase distribution is age dependent, whereas total amylase activity shows no correlation with age.

scholarly journals Isoelectric points of erabutoxins and monoacyl derivatives of erabutoxin b. Estimation of the pK values of amino groups in erabutoxins by using isoelectric-focusing data

1982 ◽  
Vol 203 (2) ◽  
pp. 427-433 ◽  
Author(s):  
N UI ◽  
C Takasaki ◽  
N Tamiya
Keyword(s):  
Isoelectric Focusing ◽  
Isoelectric Point ◽  
Amino Group ◽  
Amino Groups ◽  
Sea Snake ◽  
Isoelectric Points ◽  
Point Data ◽  
Laticauda Semifasciata ◽  
Erabutoxin B ◽  
Derivatives Of

The isoelectric points of erabutoxins a, b and c, neurotoxic proteins of a sea snake, Laticauda semifasciata, were determined by density-gradient isoelectric focusing. The same measurement was also made with monoacyl derivatives of erabutoxin b, in which each one of all amino groups had been either acetylated or propionylated. Erabutoxins a and b showed the same isoelectric point at pH 9.68. The values for [1-N alpha-acetyl-arginine]-, [15-N6-acetyl-lysine]-, [27-N6-acetyl-lysine]-, [47-N6-propionyl-lysine]- and [51-N6-acetyl-lysine]-erabutoxin b were at pH 9.52, 9.31, 9.45, 9.22 and 9.09 respectively, being definitely different from each other and lower than the value for the unmodified molecule. The isoelectric point of erabutoxin c, which is [51-asparagine]-erabutoxin b, was the same as that of [51-N6-acetyl-lysine]erabutoxin b. Assuming that no change in pK occurs on monoacylation, the pK values of amino groups in erabutoxin b were calculated from the isoelectric-point data. It is indicated that the pK values of zeta-amino groups differ markedly from each other and that the value of alpha-amino group is anomalously high.

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