Bong-Keun Choi
Kyung Hee University · Medicine
About the Lab
Professor Bong-Keun Choi's research lab specializes in clinical biochemistry and immunology, with a primary focus on prostate-specific antigen and acid phosphatase (PAP) as tumor markers. The lab has made significant contributions to the immunological characterization, purification, and assay development of prostatic acid phosphatase, including its isozymic forms and antigenic specificity. Research also extends to growth standards in pediatrics and radiation-induced bone complications in gynecological oncology, reflecting a multidisciplinary approach combining clinical diagnostics with molecular immunology. The lab's work has advanced the understanding of tumor markers and their application in cancer diagnosis and monitoring.
Research Overview
Research Output Trend
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Selected Papers
15Purpose : Since 1967, The Korean Pediatric Society and Korean Government have developed Korean Growth Standards every 10 years. Last version was published in 1998. During past 40 years, Korean Growth Standards were mainly descriptive charts without any systematic nor statistical standardization. With the global epidemic of obesity, many authorities such as World Health Organization (WHO) and United States' Centers for Disease Control (CDC) have been changed their principles of growth charts to c
Radiation-induced pelvic insufficiency fractures are a frequent complication of radiation therapy for uterine cervical cancer. Osteolysis and avascular necrosis of the femoral head were also diagnosed using MRI after radiation therapy.
The immunologic specificity of human prostatic acidphosphatase has been established by several previous investigations as well as in this study. An apparent exception to this specificity was observed--a case of pancreatic islet cell carcinoma metastasized to the liver produced acid phosphatase that was immunologically indistinguishable from the prostatic acid phosphatase. In this case, the possibility of prostatic involvement was convincingly ruled out by clinical follow-ups and by postmortem pa
Human prostatic acid phosphatase (orthophosphoric monoester phosphohydrase, EC 3.1.3.2) is purified to homogeneity by standard procedures which include CM-Sephadex, Con A affinity chromatography and gel filtration. The purified enzyme is antigenically specific and has a M.W. of 100,000 with subunit M.W. of 48,000. However, the enzyme exhibited charge heterogeneity. Two major electrophoretic or chromatographic isozymic forms of PAP were separated by DEAE-Sephadex chromatography and their immunoch
A double-antibody radioimmunoassay method for prostate-specific acid phosphatase (PAP) is presented. Experimental details are outlined to assess the reproducibility and reliability of the method under assay conditions. The upper limit of the serum PAP levels in the present assay was set at 2.4 ng/100 microliter by 162 determinations of normal serum samples. The serum PAP levels of patients with nonprostatic malignant tumors fell in the normal range, whereas the levels higher than 4.0 ng/100 micr
Immunologic specificity of the prostatic acid phosphatase (PAP) and the kinetics of the PAP-anti-PAP antibody interactions were studied in detail. Antigenic identity of electrophoretic isozymes of PAP was established in this study. Counterimmunoelectrophoretic assay, radioimmunoassay, and immunofluorescence technique were developed to detect PAP and PAP-synthesizing cells. These techniques were applied to the determination of serum PAP levels and to the identification of metastatic prostate canc
Human prostatic acid phosphatase [PAP] is antigenically uniquely different from acid phosphatases of other tissue origins. Nevertheless, a small degree of antigenic cross-reactivity between PAP and other lysosomal acid phosphatase(s) [LAP] has been suspected. In order to resolve this question, we have adopted two approaches: one involving structural studies by peptide mapping, and the other involving topological mapping through the use of uniquely defined antibodies. Purified PAP was dissociated
We compare the double-antibody radioimmunoassay (RIA) and immunoenzyme assay (IEA) for measuring the concentration of prostatic acid phosphatase in human serum. Experimental details and assay performance of the two methods are outlined. Mean values for 385 normal persons were 1.02 (SD 1.32) microgram/L by IEA, 2.69 (SD 1.8) microgram/L by RIA. Results of the two methods was highly correlated [r = 0.9813, y(RIA) = 0.35 x (IEA) + 0.42, p < 0.001]. If we choose x- + 2 SD as the normal range, 3-10%
Abstract We compare the double-antibody radioimmunoassay (RIA) and immunoenzyme assay (IEA) for measuring the concentration of prostatic acid phosphatase in human serum. Experimental details and assay performance of the two methods are outlined. Mean values for 385 normal persons were 1.02 (SD 1.32) microgram/L by IEA, 2.69 (SD 1.8) microgram/L by RIA. Results of the two methods was highly correlated [r = 0.9813, y(RIA) = 0.35 x (IEA) + 0.42, p &lt; 0.001]. If we choose x- + 2 SD as the norm
Human sera or plasma containing acid phosphatases were mixed with rabbit antiserum specific for prostatic acid phosphatase (PAP) and the resulting primary immune complexes were precipitated by ammonium sulfate. The amount of specifically precipitated PAP was estimated directly by its enzyme activity. Using this assay, as little as 10 ng/ml of the PAP could be determined. Excellent correlation of this assay method with other immunoassays of PAP was demonstrated.
Natural killer (NK) cell activity of prostatic cancer patients was compared with that of control groups by the radioactive indium (111In) release assay using the K562 and H494 cells as targets. Patients suffering from advanced prostatic cancer (clinical stages C and D) exhibited significantly lower NK activity against K562 cells (28 +/- 18%) than did the normal group (41 +/- 19%). The lower NK activity of these patients is not related to their age, since patients in the same age range with local
Research Areas
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