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Therapeutic Methods and Therapies TCIM
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1.
Explore (NY) ; 19(6): 832-841, 2023.
Article in English | MEDLINE | ID: mdl-37353458

ABSTRACT

CONTEXT: Shoulder disorders impair the ability to work. In most cases, the primary symptoms caused by shoulder disorders consist of pain and limitations in the range of motion. OBJECTIVES: This study aimed to investigate the efficacy of motion style acupuncture treatment (MSAT), a conservative treatment modality for shoulder disorders. DESIGN: prospective observational study SETTING: A Korean Medicine hospital PATIENTS: Eighty outpatients with shoulder disorders INTERVENTION: Either MSAT with integrative Korean medicine treatment (MSAT group; n = 40) or integrative Korean medicine treatment only (control group; n = 40). OUTCOME MEASURES: The primary outcome was the shoulder range of motion (ROM), and the secondary outcomes were the numeric rating scale (NRS), visual analog scale (VAS), shoulder pain and disability index (SPADI), and 5-level EuroQol 5-dimension (EQ-5D-5L) scores. RESULTS: At the primary endpoint (2 weeks from the start of the treatment), the MSAT group showed statistically significantly larger ROM for all motions, except adduction ROM, compared to the control group [Flexion ROM (165.10±4.14 vs. 150.49±4.06; P<0.001), extension ROM (43.24±1.55 vs. 40.56±1.51; P<0.05), abduction ROM (160.92±5.68 vs. 134.95±5.54; P<0.001), internal rotation ROM (73.38±2.96 vs. 65.00±2.89; P<0.001), and external rotation ROM (73.78±3.61 vs. 65.88±3.50; P<0.01)]. Additionally, the MSAT group showed significantly lower NRS, SPADI scores at week 2 than the control group; this trend was maintained until the 3-month follow-up.


Subject(s)
Acupuncture Therapy , Shoulder Joint , Humans , Shoulder , Shoulder Pain/therapy , Prospective Studies , Acupuncture Therapy/adverse effects , Range of Motion, Articular , Treatment Outcome
2.
Int J Food Sci Nutr ; 60 Suppl 2: 150-61, 2009.
Article in English | MEDLINE | ID: mdl-19462329

ABSTRACT

Adenophora triphylla is commonly used in food materials and oriental medicine as an analgesic, anti-inflammatory, and antitussive. In the present study, the leaves and roots of A. triphylla were extracted with water and ethanol, respectively, to examine the extracts' in vitro antioxidant activities and total phenolic contents, as well as A. triphylla's potential as a new functional food source and safe and inexpensive supply of antioxidants. Different antioxidant tests were employed and the results were compared with ascorbic acid as a standard antioxidant. The total extractable contents of phenolic compounds and flavonoids, which relate to antioxidant activity in medicinal plants, were also measured. The leaf extracts had notable levels of total phenolics and flavonoids and showed high radical and nitrite scavenging activities as well as inhibition activity against enzymes that induce oxidation. These results suggest that A. triphylla leaves are a potential ingredient for food supplements and a natural source of antioxidants.


Subject(s)
Antioxidants/analysis , Campanulaceae/chemistry , Flavonoids/pharmacology , Functional Food , Phenols/pharmacology , Plant Leaves/chemistry , Plant Roots/chemistry , Analgesics/pharmacology , Anti-Inflammatory Agents/analysis , Anti-Inflammatory Agents/pharmacology , Antioxidants/pharmacology , Antitussive Agents/analysis , Antitussive Agents/pharmacology , Diet , Flavonoids/analysis , Free Radical Scavengers/analysis , Free Radical Scavengers/pharmacology , Humans , Phenols/analysis , Plant Extracts/chemistry , Plant Extracts/pharmacology
3.
J Med Food ; 8(4): 462-8, 2005.
Article in English | MEDLINE | ID: mdl-16379556

ABSTRACT

An alkaline serine protease that hydrolyzes soybean protein into strong angiotensin I-converting enzyme inhibitory hydrolysates was isolated from alkalophilic Bacillus sp. SS103 and purified. The enzyme was purified by ammonium sulfate precipitation followed by gel filtration, cationic exchange column chromatography, and anionic exchange column chromatography. When run on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing gel, the purified enzyme gave a 36-kDa band and pI 5.5, respectively. The enzyme showed maximum activity at pH 11.0 and 50 degrees C. This enzyme activity was highly inhibited by aprotinin, suggesting it belongs to the serine protease class of enzymes. The K (m) and V (max) of the enzyme, when casein was used for the substrate, were 9.7 x 10-4 mM and 244 microg/minute, respectively. From the results of this study, it is concluded that the purified alkaline protease isolated from Bacillus sp. SS103 should be further studied for production of biofunctional hydrolysates.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors , Bacillus/enzymology , Serine Endopeptidases/isolation & purification , Serine Endopeptidases/metabolism , Soybean Proteins/metabolism , Soybean Proteins/pharmacology , Amino Acids/analysis , Aprotinin/pharmacology , Chemical Fractionation , Chromatography , Electrophoresis, Polyacrylamide Gel , Enzyme Stability , Hydrogen-Ion Concentration , Isoelectric Point , Kinetics , Molecular Weight , Serine Endopeptidases/chemistry , Serine Proteinase Inhibitors/pharmacology , Temperature
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