ABSTRACT
The thyroid is resistant to infection due to its anatomical and physiological characteristics. We present a rare case of invasive liver abscess with metastatic thyroid abscess and endogenous endophthalmitis in a previously healthy 55-year-old female patient without diabetes or other medical illness. This report raises an important question of the virulence of Klebsiella pneumoniae as an increasingly common causative agent of liver abscess.
Subject(s)
Endophthalmitis/diagnosis , Klebsiella Infections/diagnosis , Anti-Bacterial Agents/therapeutic use , Endophthalmitis/etiology , Female , Humans , Klebsiella Infections/complications , Klebsiella Infections/drug therapy , Klebsiella pneumoniae/isolation & purification , Liver Abscess/complications , Liver Abscess/diagnosis , Middle Aged , Thyroid Gland/diagnostic imaging , Thyroid Gland/pathology , Tomography, X-Ray Computed , UltrasonographyABSTRACT
PURPOSE: This purpose of this study was to develop and validate a Self-Efficacy Scale for Self-Management of Breast Cancer (SESSM-B). METHODS: The SESSM-B was developed and validated as follows: Item generation, pilot study, and tests of validity and reliability. Twenty-one items were developed through evaluation by 10 experts and 13 items were finally confirmed through item analysis and factor analysis. Psychometric testing was performed with a convenience sample of 303 women with breast cancer. Data were analyzed using factor analysis, Pearson correlation coefficients, and Cronbach's alpha. RESULTS: Five factors evolved from the factor analysis, which explained 69.8% of the total variance. The first factor 'coping with psycho-informational demand' explained 17.2%, 2nd factor 'maintenance of healthy lifestyle' 14.5%. 3rd factor 'management of side-effects' 13.3%, 4th factor 'therapeutic compliance' 12.8%, and 5th factor 'sexual life' 11.9%. SESSM-B also demonstrated a concurrent validity with health-related quality of life scale, EORTC QLQ-C30 & BR23. The internal consistency, Cronbach's alpha, was .78, and reliability of the subscales ranged from .61 to .79. CONCLUSION: The results of this study suggest that the SESSM-B is an easy, reliable, and valid instrument to measure self-efficacy for self-management of breast cancer.
Subject(s)
Breast Neoplasms/psychology , Self Care , Self Efficacy , Adaptation, Psychological , Adult , Factor Analysis, Statistical , Female , Health Status , Humans , Middle Aged , Pilot Projects , Program Development , Psychometrics , Quality of Life , Surveys and QuestionnairesABSTRACT
A gene (astA) encoding arylsulfate sulfotransferase (ASST), which transfers a sulfate group from phenolic sulfate esters to phenolic acceptors, was cloned from a Eubacterium A-44 genomic library. The probe (1.5 kb fragment) for the astA gene was prepared from the PCR product of the primers produced using two internal amino acid sequences of ASST, which had been purified from Eubacterium A-44. The astA gene was cloned into the pKF3 vector. Its sequence revealed a 1863 bp open reading frame (ORF) encoding a protein containing 620 amino acids with a secretary signal peptide, and showed 91% homology (identity) to Eubacterium rectale IIIH previously reported. The cloned astA gene was expressed under the T7 promoter of the expression vectors, pET-39b(+) and pET-26b(+), in Escherichia coli BL21 (DE3), and the expressed ASSTs were purified using His Bind column chromatography. The specific activities of the purified ASSTs were 25.6 micromol/min/mg and 37.1 micromol/min/mg, respectively.
Subject(s)
Arylsulfotransferase/biosynthesis , Arylsulfotransferase/isolation & purification , Bacterial Proteins/biosynthesis , Bacterial Proteins/isolation & purification , Eubacterium/enzymology , Amino Acid Sequence , Arylsulfotransferase/genetics , Arylsulfotransferase/metabolism , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Base Sequence , Chromatography, Affinity/methods , Cloning, Molecular , Escherichia coli/genetics , Gene Library , Industrial Microbiology/methods , Molecular Sequence Data , Parabens/metabolism , Polymerase Chain Reaction/methods , Recombinant Proteins/biosynthesis , Sequence Alignment , Sequence Analysis, Protein , Sequence Analysis, RNA , Substrate Specificity , Transformation, Bacterial , Tyramine/metabolism , Tyrosine/metabolismABSTRACT
Two novel chondroitinases, chondroitin ABC lyase (EC 4.2.2.4) and chondroitin AC lyase (EC 4.2.2.5), have been purified from Bacteroides stercoris HJ-15, which was isolated from human intestinal bacteria with glycosaminoglycan degrading enzymes. Chondroitin ABC lyase was purified to apparent homogeneity by a combination of QAE-cellulose, CM-Sephadex C-50, hydroxyapatite and Sephacryl S-300 column chromatography with a final specific activity of 45.7 micromol.min-1.mg-1. Chondroitin AC lyase was purified to apparent homogeneity by a combination of QAE-cellulose, CM-Sephadex C-50, hydroxyapatite and phosphocellulose column chromatography with a final specific activity of 57.03 micromol.min-1.mg-1. Chondroitin ABC lyase is a single subunit of 116 kDa by SDS/PAGE and gel filtration. Chondroitin AC lyase is composed of two identical subunits of 84 kDa by SDS/PAGE and gel filtration. Chondroitin ABC and AC lyases showed optimal activity at pH 7.0 and 40 degrees C, and 5.7-6.0 and 45-50 degrees C, respectively. Both chondroitin lyases were potently inhibited by Cu2+, Zn2+, and p-chloromercuriphenyl sulfonic acid. The purified Bacteroidal chondroitin ABC lyase acted to the greatest extent on chondroitin sulfate A (chondroitin 4-sulfate), to a lesser extent on chondroitin sulfate B (dermatan sulfate) and C (chondroitin 6-sulfate). The purified chondroitin AC lyase acted to the greatest extent on chondroitin sulfate A, and to a lesser extent on chondroitin C and hyaluronic acid. They did not act on heparin and heparan sulfate. These findings suggest that the biochemical properties of these purified chondroitin lyases are different from those of the previously purified chondroitin lyases.
