No abstract available.
Electrophoresis, Polyacrylamide Gel* ; Proteinuria*

No abstract available.
Clostridium difficile* ; Clostridium* ; Electrophoresis, Polyacrylamide Gel*

No abstract available.
Clostridium difficile* ; Clostridium* ; Electrophoresis, Polyacrylamide Gel*

We investigated the biochemiesl change of keratin by the methods of SDS-PAGE and Two-dimensional gel electrophoresis, and observed electron microscopic ultrestructural changes in five Unna-Thost palmoplantar keratoderma patients and two normal adults. The results are summarized as follows : 1. The increased bands of 51 kd and newly appearing 48 kd, 56 kd keratins were observed on the SDS-PAGE and compared to the normsl control. 2. The newly appearing 48 kd(acidic) paired with 56 kd(basic) keratins and 51 kd keratin and the disappearance of 59 kd(basic), 64 kd(basic) keratins were observed on the two-dimensional gel electrophoresis and compared to the normal control. 3. The variable sized, numerous, globular, irregularly beam-shaped and granular kerstohyaline granules were scattered in the granular cell and corneocyte. Numerous ribosomes were noted between the clumped tonofibrils and around the keratohyaline granules. The lipid droplets were seen in the corneocytes and granular cells on the electron microscope.
Adult ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Humans ; Keratoderma, Palmoplantar* ; Ribosomes

In this study,the protein in different Cordyceps samples,which include fresh sample( S1),22 ℃ drying sample( S2),37 ℃ drying sample( S3) and 60 ℃ drying sample( S4),were analyzed by sodium dodecylsupinate-polyacrylamide gel electrophoresis( SDS-PAGE) and two-dimensional electrophoresis( 2-DE). The total protein contents in Cordyceps samples were from 1. 655-4. 493 mg·g~(-1) and the protein contents in fresh sample was the highest. The results of SDS-PAGE showed that the mainly ranges of protein molecular weight of Cordyces samples were 10-100 kDa and the numbers of protein bands were 28 to 41,the fresh sample had the maximum number of protein bands. The 2-DE profiles were analyzed by PDQuest software. The resulted indicated that 488-876 protein spots were detected in different Cordyceps samples and the isoelectric point( pI) was distributed between 4. 5 and 6. 5,the protein molecular weight was distributed in 10-20 kDa and 25-100 kDa,the fresh sample had the maximum number of protein spots. Therefore,the drying process could decrease contents and species of protein in Cordyceps,and the different drying conditions had different effects on protein. These results provide a reference for improving the drying process of Cordyceps.
Cordyceps ; chemistry ; Desiccation ; methods ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins ; analysis ; Molecular Weight

BACKGROUND: The present study was done to evaluate the usefulness of SDS-PAGE in measuring glomerular proteins and tubular proteins in patients with type I DM without overt proteinuria. METHODS: The study population consisted of 76 children with type I DM who have been participated in the Taegu Diabetic Camp from 1997 to 2000. We measured urine albumin, NAG, beta2-microglobulin, creatinine level in urine samples collected for 12 hours in 22 children and simultaneously we analyzed urinary proteins by SDS-PAGE. In remainder 54 children, we measured urine albumin, NAG, creatinine level in random morning urines and urinary proteins by SDS-PAGE. RESULTS: In 22 of 76 children, urinary albumin-to-creatinine ratio (mg/mg), NAG (U/g) and beta2-microglobulin (microgram/g) were 0.021, 2.99 and 170.2, respectively. Positive correlation between urine albumin and NAG was statistically significant (r=0.51, p< 0.05). No significant relations between urinary proteins, such as albumin, NAG, beta2-microglobulin, and clinical characteristics, such as age, duration of illness, HbA1c, were observed. In diagnosing `microalbuminuria', sensitivity of SDS-PAGE was 63% and band of tubular proteins was not detected in any children. CONCLUSION: We thought that SDS-PAGE could be one of useful methods in diagnosing early stage of diabetic nephropathy. The more large scale study is necessary.
Child* ; Creatinine ; Daegu ; Diabetic Nephropathies ; Electrophoresis, Polyacrylamide Gel* ; Humans ; Proteinuria*

No abstract available.
Electrophoresis, Polyacrylamide Gel* ; Immunoblotting* ; Korea* ; Rickettsia typhi* ; Rickettsia*

OBJECTIVETo study the interactions between hemoglobin (Hb) and other proteins within human erythrocytes by using the electrophoresis release test (ERT) and co-immunoprecipitation.

METHODSFirst, the fresh normal adult anti-coagulated whole blood was washed to prepare packed RBCs, which were further prepared to erythrocyte suspension and hemolysate.The erythrocyte suspension and hemolysate were analyzed by the electrophoresis release test (ERT) at the same time, and then the band of HbA of erythrocyte sample (RA) and the corresponding band of hemolysate sample (HA) were cut out from the gel and were enriched by freeze-thaw method. Then, the samples were bound with hemoglobin β antibody (37-8) AC, the complexes were separated through 5%-12% SDS-PAGE followed by Q-TOF.

RESULTSFive bands were found in the gel, each of which was treated by hemoglobin β antibody (37-8) AC, the protein bands of 16,20,22,28 and 50 kD were emerged in RA, HA and RBC lysis.The bands were identified by MS, and the results showed that these bands were hemoglobin, band 3, peroxiredoxin2 (Prx2), band 3 and β-actin, band 3 respectively.

CONCLUSIONHbA may interact with Prx2, Band 3 and β-actin, and then the complexes are formed with each other within erythrocytes.

No abstract available.
Blood Platelets* ; Electrophoresis, Polyacrylamide Gel* ; Membrane Glycoproteins* ; Membranes* ; Thrombasthenia*

The biological interpretation of two-dimensional (2D) gel electrophoresis experiments is a key step toward understanding the functions of biological systems. We here present a web-based integrated database, called 2DSpotDB, for the management of proteome data derived from several pathogens. The 2DSpotDB was established as a part of the management of a pathogen proteome project at the Korea National Institute of Health. The goals of the 2DSpotDB implementation are to store and define important pathogen genes, retrieve information obtained by 2D polyacrylamide gel electrophoresis and mass spectrometry, and create an integrated system to provide pathogen proteome information for biological scientists. This database currently contains 14 gels and information on 387 protein spots, among which 329 proteins were identified and annotated.
Acrylic Resins ; Data Mining ; Electrophoresis ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Gels ; Korea ; Mass Spectrometry ; Proteins ; Proteome