PubMed Health⌕ Search

Biomedical subjects

B Hong

Publications and source records attributed to B Hong.

At least 55 records · Page 3Linked to original sources
PubMed1998

[Secretory expression of salmon calcitonin in Streptomyces lividans].

A gene coding for salmon calcitonin precursor (sCT-Gly) was amplified from salmon genomic DNA by Polymerase Chain Reaction (PCR) and fused to the expression and secretion signals of melC1 amplified by PCR. The fusion gene was cloned into the Streptomyces vector pIJ680 and expressed under the control of aminoglycoside phosphotransferase gene (aph) promoter. Streptomyces lividans TK54 transformed with the expression plasmid (pMS680) secreted biologically active sCT-Gly into the culture medium which was confirmed by Enzyme Immunoassay (EIA) and bioassay. Production of sCT-Gly by the recombinant strain in YEME medium reached a maximum of 100 micrograms/L culture at about 96 h. The recombinant sCT-Gly had almost the same HPLC retention time as the standard sCT obtained from Sigma.

Calcitonin↗
PubMed1998

[Malakoplakia of the prostate].

OBJECTIVE: To study the diagnosis and treatment of prostatic malakoplakia. METHOD: Two cases of malakoplakia were reported, and the cases and articles were reviewed. RESULT: The disease is an inflammation of the prostate, and lower immunocompetence is concomitance. The patients had symptoms of dysuria and urethralgia. The tubercle could be found. Pathological section revealed malakoplakia cells and Michaelis-Gutman inclusion bodies. Many patients were performed radical prostatectomy because of misdiagnosis. CONCLUSION: Biopsy of the prostate and antibiotics should be used clinically.

Humans↗
PubMed1998

[Characterization of the Streptomyces plasmid pSGL1].

The plasmid pSGL1(7.4 kb) which was isolated from antitumor antibiotic C-1027 producing strain Streptomyces globisporus C-1027 was characterized. It could be introduced into Streptomyces lividans by transformation. Following a series of deletion experiments, the minimal replication region was located within a 2.0 kb Sau 3AI fragment. pSGL1 is compatible with pIJ101. pSGL1 and its derivatives have a copy number of 70-250. Some of the derived plasmids such as pSGLN and pSGLS3 have suitable selectable antibiotic resistance marker and unique restriction endonuclease sites and may be potentially useful as cloning vectors. These plasmids may be used to design and construct efficient secretory expression vectors.

Aminoglycosides↗
PubMed1997

A novel procedure for the extraction of protein deposits from soft hydrophilic contact lenses for analysis.

PURPOSE: A quick, simple, and efficient extraction technique was developed for the removal of protein from soft hydrophilic contact lenses. METHODS: An extraction solvent consisting of a 50:50 mix of 0.2% trifluoroacetic acid and acetonitrile was used to remove protein from in vitro laboratory-deposited and human-worn contact lenses. The protein removed was analyzed using HPLC, bicinchoninic acid (BCA) analysis, and SDS-PAGE gel electreophoresis. RESULTS: Extraction efficiency for lysozyme from laboratory-deposited Group IV lenses was determined to be approximately 100%. Group IV human-worn contact lenses were extracted and analyzed for lysozyme by HPLC and total protein by bicinchoninic acid (BCA) analysis. Groups I, II, III, and IV contact lenses deposited with an artificial tear protein solution and human-worn lenses were extracted and analyzed by SDS-PAGE gel electreophoresis and micro-BCA. CONCLUSIONS: The ACN/TFA procedure offers a simple, quick, and efficient extraction technique for removal of protein from contact lenses for subsequent analysis.

Acetonitriles↗
PubMed1997

Nop2p is required for pre-rRNA processing and 60S ribosome subunit synthesis in yeast.

To investigate the function of the nucleolar protein Nop2p in Saccharomyces cerevisiae, we constructed a strain in which NOP2 is under the control of a repressible promoter. Repression of NOP2 expression lengthens the doubling time of this strain about fivefold and reduces steady-state levels of 60S ribosomal subunits, 80S ribosomes, and polysomes. Levels of 40S subunits increase as the free pool of 60S subunits is reduced. Nop2p depletion impairs processing of the 35S pre-rRNA and inhibits processing of 27S pre-rRNA, which results in lower steady-state levels of 25S rRNA and 5.8S rRNA. Processing of 20S pre-rRNA to 18S rRNA is not significantly affected. Processing at sites A2, A3, B1L, and B1S and the generation of 5' termini of different pre-rRNA intermediates appear to be normal after Nop2p depletion. Sequence comparisons suggest that Nop2p may function as a methyltransferase. 2'-O-ribose methylation of the conserved site UmGm psi UC2922 is known to take place during processing of 27S pre-rRNA. Although Nop2p depletion lengthens the half-life of 27S pre-RNA, methylation of UmGm psi UC2922 in 27S pre-rRNA is low during Nop2p depletion. However, methylation of UmGm psi UC2922 in mature 25S rRNA appears normal. These findings provide evidence for a close interconnection between methylation at this conserved site and the processing step that yields the 25S rRNA.

Amino Acid Sequence↗
PubMed1996

Monitoring of soluble HLA alloantigens and anti-HLA antibodies identifies heart allograft recipients at risk of transplant-associated coronary artery disease.

The development of accelerated transplant-related coronary artery disease (T-CAD) is the major obstacle to long-term survival of cardiac allografts. We have investigated the role of various demographic and immunologic parameters as prognostic indicators of T-CAD in a population of 274 heart allograft recipients. Our data demonstrate that patients who experience more than 1 episode of acute rejection per year and/or develop antidonor HLA antibodies are at increased risk of developing T-CAD. Using HLA-A2 as a marker for the release of soluble HLA antigens from the donor, we established that recipients displaying circulating donor alloantigens for more than 26 weeks following transplantation are at increased risk of developing T-CAD (P=0.008). This association suggests that the release of alloantigens from the allograft is indicative of chronic injury and/or that it stimulates chronic rejection via the indirect allorecognition pathway. Our findings indicate that patients at risk of developing T-CAD can be identified by monitoring the release of donor alloantigens and production of antidonor HLA antibodies following transplantation.

Adolescent↗
PubMed1996

Targeting of two Arabidopsis H(+)-ATPase isoforms to the plasma membrane.

More than 11 different P-type H(+)-ATPases have been identified in Arabidopsis by DNA cloning. The subcellular localization for individual members of this proton pump family has not been previously determined. We show by membrane fractionation and immunocytology that a subfamily of immunologically related P-type H(+)-ATPases, including isoforms AHA2 and AHA3, are primarily localized to the plasma membrane. To verify that AHA2 and AHA3 are both targeted to the plasma membrane, we added epitope tags to their C-terminal ends and expressed them in transgenic plants. Both tagged isoforms localized to the plasma membrane, as indicated by aqueous two-phase partitioning and sucrose density gradients. In contrast, a truncated AHA2 (residues 1-193) did not, indicating that the first two transmembrane domains alone are not sufficient for plasma membrane localization. Two epitope tags were evaluated: c-myc, a short, 11-amino acid sequence, and beta-glucuronidase (GUS), a 68-kD protein. The c-myc tag is recommended for its sensitivity and specific immunodetection. GUS worked well as an epitope tag when transgenes were expressed at relatively high levels (e.g. with AHA2-GUS944); however, evidence suggests that GUS activity may be inhibited when a GUS domain is tethered to an H(+)-ATPase complex. Nevertheless, the apparent ability to localize a GUS protein to the plasma membrane indicates that a P-type H(+)-ATPase can be used as a delivery vehicle to target large, soluble proteins to the plasma membrane.

Amino Acid Sequence↗
PubMed1995

Analysis of C-Ha-ras gene amplification and mutation in laryngeal carcinoma.

In order to study the altered molecular events during laryngeal carcinogenesis and elucidate the role of Ha-ras oncogene amplification and mutation, we have examined their profile by polymerase chain reaction (PCR) and selective oligonucleotide hybridization. We analyzed the mutational status of codon 12 of Ha-ras in 22 laryngeal carcinomas and 10 normal tissues, and found that 7 of 22 laryngeal carcinomas contained a Ha-ras mutation at codon 12. The frequency of mutation was 32%. None of the normal tissues revealed mutation. Moreover, no amplification was found in cancers when compared to the normal. Our findings indicated that the activated Ha-ras gene existed in laryngeal carcinoma, and activation of the Ha-ras gene by mutation at codon 12 might play a key role in laryngeal carcinogenesis.

Carcinoma, Squamous Cell↗
PubMed1994

Yeast NOP2 encodes an essential nucleolar protein with homology to a human proliferation marker.

We have isolated a gene (NOP2) encoding a nucleolar protein during a search for previously unidentified nuclear proteins in the yeast Saccharomyces cerevisiae. The protein encoded by NOP2 (Nop2p) has a predicted molecular mass of 70 kD, migrates at 90 kD by SDS-PAGE, and is essential for cell viability. Nop2p shows significant amino acid sequence homology to a human proliferation-associated nucleolar protein, p120. Approximately half of Nop2p exhibits 67% amino acid sequence identity to p120. Analysis of subcellular fractions indicates that Nop2p is located primarily in the nucleus, and nuclear fractionation studies suggest that Nop2p is associated with the nucleolus. Indirect immunofluorescence localization of Nop2p shows a nucleolar-staining pattern, which is heterogeneous in appearance, and a faint staining of the cytoplasm. The expression of NOP2 during the transition from stationary phase growth arrest to rapid growth was measured, and compared to the expression of TCM1, which encodes the ribosomal protein L3. Nop2p protein levels are markedly upregulated during the onset of growth, compared to the levels of ribosomal protein L3, which remain relatively constant. NOP2 mRNA levels also increase during the onset of growth, accompanied by a similar increase in the levels of TCM1 mRNA. The consequences of overexpressing NOP2 from the GAL10 promoter on a multicopy plasmid were investigated. Although NOP2 overexpression produced no discernible growth phenotype and had no effect on ribosome subunit synthesis, overexpression was found to influence the morphology of the nucleolus, as judged by electron microscopy. Overexpression caused the nucleolus to become detached from the nuclear envelope and to become more rounded and/or fragmented in appearance. These findings suggest roles for NOP2 in nucleolar function during the onset of growth, and in the maintenance of nucleolar structure.

Amino Acid Sequence↗