scholarly journals Underglycosylation of IgA1 Hinge Plays a Certain Role for Its Glomerular Deposition in IgA Nephropathy

1999 ◽  
Vol 10 (4) ◽  
pp. 760-769
Author(s):  
YOSHIYUKI HIKI ◽  
TOHRU KOKUBO ◽  
HITOO IWASE ◽  
YOSHIHIKO MASAKI ◽  
TAKASHI SANO ◽  
...  
Keyword(s):  
Iga Nephropathy ◽  
Gas Phase ◽  
Wistar Rats ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Peanut Agglutinin ◽  
Vicia Villosa ◽  
High Affinity ◽  
Fraction H ◽  
Peptide Antibody

Abstract. This study was performed to isolate and investigate the IgA1 that could accumulate in glomeruli (glomerulophilic IgA1). IgA1 was fractionated by the electric charge and the reactivity to Jacalin. Serum IgA1 of IgA nephropathy patients was separated and fractionated using a Jacalin column and subsequent ion-exchange chromatography. The fractions were divided into three groups of relatively cationic (C), neutral (N), and anionic (A). IgA1 was also divided into Jacalin low (L), intermediate (I), and high (H) affinity fractions by serial elution using 25, 100, and 800 mM galactose. The left kidneys of Wistar rats were perfused with 2, 5, or 10 mg of each group of IgA1. The rats were sacrificed 15 min, 30 min, 3 h, or 24 h after the perfusion. The accumulation of each IgA1 in the glomeruli was then observed by immunofluorescence. The IgA1 of the fractions N and H separated by the two methods was definitely accumulated in the rat glomeruli with a similar pattern. The electrophoresis revealed that the macromolecular IgA1 was increased in fraction H compared with other fractions. Therefore, Jacalin high-affinity IgA1 (fraction H) was applied on a diethylaminoethyl column and divided into electrically cationic (HC), neutral (HN), and anionic (HA). Only the asialo-Galβ1,3GalNAc chain was identified in the fraction HN IgA1 by gas-phase hydrazinolysis. Furthermore, the IgA1 fraction was strongly recognized by peanut agglutinin, Vicia Villosa lectins, and antisynthetic hinge peptide antibody. These results indicated that the IgA1 molecules having the underglycosylated hinge glycopeptide played a certain role in the glomerular accumulation of IgA1 in IgA nephropathy.

Hemoglobin Solutions Coupled with Polyethylene Glycol 1900: Preparation, Purification, Quality Control and Pharmacological Trials by Hemorrhagic Shock

1988 ◽  
Vol 11 (5) ◽  
pp. 393-402 ◽  
Author(s):  
P. Labrude ◽  
P. Mouelle ◽  
P. Menu ◽  
C. Vigneron ◽  
E. Dellacherie ◽  
...  
Keyword(s):  
Hemorrhagic Shock ◽  
Heme Proteins ◽  
Wistar Rats ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Hemoglobin ◽  
Chemical Modifications ◽  
Short Term ◽  
High Affinity ◽  
Comparative Results

The usefulness of hemoglobin solutions as oxygen transporters is limited by their high affinity for oxygen and rapid elimination from the circulation. Various chemical modifications of hemoglobin aimed at overcoming these two handicaps have been suggested. We have developed a conjugate of pyridoxylated human hemoglobin with monomethoxypolyoxyethylene 1900, whose preparation and properties are described. We present comparative results on short-term or definitive survival of Wistar rats which, during hemorrhagic shock due to the loss of 60 or 80% of their blood mass, were given a solution of native or modified hemoglobin, in some cases purified by ion-exchange chromatography to remove non-heme proteins, lipids, and some endotoxins. The more complex the treatment used to improve the properties and the purity of the hemoglobin solutions, the longer the animals survived. The loss of hemoglobin in the urine was greatly reduced after conjugation: after 20 h, less than 6% of the total infused.

Identification and Distribution of m-Tyramine in the Rat

1975 ◽  
Vol 53 (1) ◽  
pp. 65-69 ◽  
Author(s):  
S. R. Philips ◽  
B. A. Davis ◽  
D. A. Durden ◽  
Alan A. Boulton
Keyword(s):  
Ion Exchange ◽  
Chromatographic Separation ◽  
Wistar Rats ◽  
Internal Standard ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mass Spectrometric ◽  
Ion Current ◽  
Mammalian Tissues ◽  
Male Wistar Rats

A procedure for the quantitative evaluation of m-tyramine in mammalian tissues is described. It involves isolation of the amine by ion-exchange chromatography, followed by conversion to the dansyl derivative, chromatographic separation, and quantitation by the mass spectrometric integrated ion current technique using an isotopically labelled internal standard. The concentrations of m-tyramine in some tissues of male Wistar rats were (mean ± S.D., nanograms per gram): brain 0.32 ± 0.03, heart 0.44 ± 0.13. kidney 12.6 ± 3.4, liver 0.27 ± 0.04, lung 0.33 ± 0.11, spleen 0.25 ± 0.07, and blood 0.15 ± 0.04.

scholarly journals Comparative study between the effects of hyaluronic acid and acid galactan purified from eggs of the mollusk Pomacea sp in wound healing

2004 ◽  
Vol 19 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Ana Katarina Menezes da Cruz ◽  
Wogelsanger Oliveira Pereira ◽  
Elizeu Antunes dos Santos ◽  
Maria Goretti Freire Carvalho ◽  
Aldo da Cunha Medeiros ◽  
...  
Keyword(s):  
Wound Healing ◽  
Small Intestine ◽  
Hyaluronic Acid ◽  
Wistar Rats ◽  
Saline Solution ◽  
Giant Cells ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Healing Tissue

PURPOSE: To compare the effect of hyaluronic acid (HA) and of AG on the healing of intestine wounds. METHODS: The semi-purified extract of the eggs of the mollusc was obtained by fractionation with ammonium sulfate and purification for ion-exchange chromatography. The obtained galactans were eluted in water (neutral galactan) and in 0.1 and 0.2M NaCl (acidic galactans). The in vivo study was performed with 45 "Wistar" rats, separated in three groups (n=15). Solutions containing HA 1%, GA 1% or saline solution 0,9%, was placed topically on the sutures of wounds in the small intestine of the rats. After 05, 10 and 21 days the animals were sacrificed and biopsy of the healing tissue was done. RESULTS: The hystologic grading was more significant for HA and AG groups when compared to the group C. AG stimulated the appearance of macrophages, giant cells and increase in the concentration of collagen in the area of the wound when compared to HA. CONCLUSION: The topical use of GA in intestinal wounds promoted the anticipation of events that are important in the wound healing.

scholarly journals Dephosphorylation of Phytate by Using theAspergillus niger Phytase with a High Affinity for Phytate

1999 ◽  
Vol 65 (10) ◽  
pp. 4682-4684 ◽  
Author(s):  
Tadashi Nagashima ◽  
Tatsuya Tange ◽  
Hideharu Anazawa
Keyword(s):  
Phytic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Aspergillus Ficuum ◽  
Michaelis Constant ◽  
High Affinity ◽  
Significant Difference

ABSTRACT A phytase (EC 3.1.3.8 ) with a high affinity for phytic acid was found in Aspergillus niger SK-57 and purified to homogeneity in four steps by using ion-exchange chromatography (two types), gel filtration, and chromatofocusing. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme gave a single stained band at a molecular mass of approximately 60 kDa. The Michaelis constant of the enzyme for phytic acid (18.7 ± 4.6 μM) was statistically analyzed. In regard to the orthophosphate released from phytic acid, a significant difference between a lowKm phytase from A. niger SK-57 and a high Km phytase from Aspergillus ficuum was recognized.

Identification and Distribution of β-Phenylethylamine in the Rat

1973 ◽  
Vol 51 (7) ◽  
pp. 995-1002 ◽  
Author(s):  
D. A. Durden ◽  
S. R. Philips ◽  
Alan A. Boulton
Keyword(s):  
Wistar Rats ◽  
Internal Standard ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mass Spectrometric ◽  
Ion Current ◽  
Mammalian Tissues ◽  
Male Wistar Rats ◽  
Dansyl Derivatives ◽  
The Brain

A procedure for the quantitative evaluation of some amines present in mammalian tissues has been developed. It includes isolation of the amines by ion exchange chromatography followed by conversion to dansyl derivatives, chromatographic separation, and quantitation by the mass spectrometric integrated ion current technique. The use of an isotopically labelled internal standard improves the precision and sensitivity of the analysis.The concentrations of β-phenylethylamine in some tissues of male Wistar rats were (ng/g); brain 1.8 ± 0.4, heart 5.7 ± 3.1, kidney 20.5 ± 2.2, liver 2.0 ± 0.7, lung 4.0 ± 1.4, and spleen 4.7 ± 2.7. In the brain the hypothalamus contained 25.3 ± 5.0, the cerebellum 3.4 ± 0.5, the stem 2.2 ± 0.9, the caudate nucleus 8.0 ± 0.3, and the 'rest' 1.1 ± 0.2 ng/g, respectively.

Identification and Distribution of p-Tyramine in the Rat

1974 ◽  
Vol 52 (5) ◽  
pp. 366-373 ◽  
Author(s):  
S. R. Philips ◽  
D. A. Durden ◽  
A. A. Boulton
Keyword(s):  
Standard Deviation ◽  
Ion Exchange ◽  
Wistar Rats ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mass Spectrometric ◽  
Ion Current ◽  
Mammalian Tissues ◽  
Male Wistar Rats ◽  
The Brain

A procedure for the quantitative evaluation of p-tyramine in mammalian tissues is described. It involves isolation of the amine by ion-exchange chromatography, followed by conversion to the dansyl derivative, chromatographic separation, and quantitation by the mass spectrometric integrated ion current technique using an isotopically labelled internal standard.The concentrations of p-tyramine in some tissues of male Wistar rats were (mean ± standard deviation (ng/g)): brain 2.0 ± 0.9, heart 3.4 ± 1.4, kidney 32.7 ± 13.1, liver 1.5 ± 0.5, lung 3.0 ± 1.2, and spleen 3.4 ± 1.2. In the brain, hypothalamus contained 11.3 ± 3.7, cerebellum 2.3 ± 1.7, stem 2.2 ± 1.0, caudate nucleus 19.2 ± 2.5, and the 'rest' 1.6 ± 0.4 ng/g, respectively.

Carnivora: The Amino Acid Sequence of the Adult European Mink (Mustela lutreola, Mustelidae) Hemoglobins

1990 ◽  
Vol 45 (3-4) ◽  
pp. 223-228 ◽  
Author(s):  
Aftab Ahmed ◽  
Meeno Jahan ◽  
Gerhard Braumtzer
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Mustela Lutreola ◽  
European Mink ◽  
Globin Chains ◽  
The Family ◽  
Insight Into

Abstract The complete amino acid sequences of the hemoglobins from the adult European mink (Mustela lutreola) are presented. The erythrocytes contain two hemoglobin components and three globin chains. The isolation of globin chains achieved by ion-exchange chromatography on a column of CM -cellulose in 8 M urea buffer. The primary structure of globin chains and of the tryptic peptides determined in liquid-and gas-phase sequenators. The alignment of the a-and β-chains with those of reported sequences from other carnivora species belonging to the family Mustelidae may give an insight into the evolution of this molecule.

Identification and Distribution of Tryptamine in the Rat

1974 ◽  
Vol 52 (6) ◽  
pp. 447-451 ◽  
Author(s):  
S. R. Philips ◽  
D. A. Burden ◽  
A. A. Boulton
Keyword(s):  
Wistar Rats ◽  
Quantitative Measurement ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ion Current ◽  
Mean Deviation ◽  
Mammalian Tissues ◽  
Male Wistar Rats ◽  
Layer Chromatography ◽  
The Brain

A procedure for the quantitative measurement of tryptamine in mammalian tissues is described. The amine is isolated by ion-exchange chromatography, converted to its dansyl derivative, further purified by thin-layer chromatography, and quantitated by the mass-spectrometric integrated ion current technique using an isotopically labelled internal standard.The concentrations of tryptamine in some tissues of male Wistar rats were (ng/g ± S.D.): brain 0.50 ± 0.07, heart 0.62 ± 0.10, kidney 8.04 ± 2.10, liver 0.73 ± 0.07, lung 0.54 ± 0.18, and spleen 0.43 ± 0.14. In the brain, the hypothalamus contained 0.94 ± 0.22, the cerebellum 0.27 ± 0.02, the stem 0.24 ± 0.06, the caudate nucleus 2.93 ± 1.14, and the "rest" 0.32 ± 0.05 ng/g (mean ± mean deviation).

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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