1.Study on Bacterial Endotoxins Test for L-Oxiracetam Injection
Hongping WANG ; Meimei HUANG ; Zuyuan RONG
China Pharmacist 2016;19(10):1993-1995
Objective:To establish a bacterial endotoxins testing method for L-oxiracetam injection. Methods: According to the gel-clot technique for bacterial endotoxin inspection and the related regulations in Chinese Pharmacopoeia (2015 edition, volume Ⅳ, general rule 1143), tachypleus amebocyte lysate (TAL) from two different manufacturers were used for bacterial endotoxins test on 3 batches of L-oxiracetam injection with methodology studies. Results:Diluted to 8. 3 mg·ml-1 , the samples showed no interference a-gainst the bacterial endotoxins test. Conclusion:The bacterial endotoxins test method for L-oxiracetam injection is applicable with the endotoxin limit of 3 EU·ml-1 .
2.Establishment of Bacterial Endotoxin Test for an Insoluble Drug Substance
Chengqian YAN ; Meimei HUANG ; Hongping WANG ; Lu ZHAO ; Zuyuan RONG ; Nan ZENG
China Pharmacist 2018;21(2):365-368
Objective:To establish the bacterial endotoxin test for HSSYO-001-3S. Methods: HSSYO-001-3S was dissolved in dimethylsulfoxide,diluted by BET water and centrifuged,and then the supernatant was used for the bacterial endotoxin test. The ex-periment was carried out according to the gel-clot technique for bacterial endotoxin inspection and the related regulations in Chinese Pharmacopoeia (2015 edition,volumeⅣ,general rule 1443). Results:HSSYO-001-3S was added with cosolvent and diluted by BET water to 1 mg·ml-1,and there was no interference effects to bacterial endotoxin test from the supernatant diluted four times or more. Conclusion:Bacterial endotoxin test can be used to control the quality of HSSYO-001-3S.
3.A novel approach for identifying the heme-binding proteins from mouse tissues.
Xiaolei LI ; Xiaoshan WANG ; Kang ZHAO ; Zhengfeng ZHOU ; Caifeng ZHAO ; Ren YAN ; Liang LIN ; Tingting LEI ; Jianning YIN ; Rong WANG ; Zhongsheng SUN ; Zuyuan XU ; Jingyue BAO ; Xiuqing ZHANG ; Xiaoli FENG ; Siqi LIU
Genomics, Proteomics & Bioinformatics 2003;1(1):78-86
Heme is a key cofactor in aerobic life, both in eukaryotes and prokaryotes. Because of the high reactivity of ferrous protoporphyrin IX, the reactions of heme in cells are often carried out through heme-protein complexes. Traditionally studies of heme-binding proteins have been approached on a case by case basis, thus there is a limited global view of the distribution of heme-binding proteins in different cells or tissues. The procedure described here is aimed at profiling heme-binding proteins in mouse tissues sequentially by 1) purification of heme-binding proteins by heme-agarose, an affinity chromatographic resin; 2) isolation of heme-binding proteins by SDS-PAGE or two-dimensional electrophoresis; 3) identification of heme-binding proteins by mass spectrometry. In five mouse tissues, over 600 protein spots were visualized on 2-DE gel stained by Commassie blue and 154 proteins were identified by MALDI-TOF, in which most proteins belong to heme related. This methodology makes it possible to globally characterize the heme-binding proteins in a biological system.
Animals
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Carrier Proteins
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biosynthesis
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genetics
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Electrophoresis, Gel, Two-Dimensional
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Electrophoresis, Polyacrylamide Gel
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Heme
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chemistry
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Hemeproteins
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biosynthesis
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genetics
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Mass Spectrometry
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Mice
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Mice, Inbred ICR
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Protein Binding
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Proteins
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chemistry
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Proteome
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Proteomics
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methods
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Sepharose
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chemistry
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Tissue Distribution