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【Were cited literature】 China Academic Journal ago 10 1 Xuwen Xiang, Pang on red, double-Shao-Min; Fluorescence Study of Hydrochlorothiazide and Human Serum Albumin [J]; Analytical Chemistry; 2004 12 2 YI Ping-Gui, Liu Junfeng, SHANG Zhi-Cai, YU Qing-Sen; fluorescence spectroscopy of methylene blue and the protein binding reaction [J]; Spectroscopy and Spectral Analysis; 2001 06 3 OF WUHAN UNIVERSITY, Tongjin Jiang, Yi Liu, Dai-Wen Pang, INSTRUMENTAL, Thermochemical ; of dipyridamole with bovine serum albumin thermodynamic characteristics of Fluorescence Spectroscopy [J]; Spectroscopy and Spectral Analysis; Sheng 2003 03 4 Good full, INSTRUMENTAL, Zhang Yan, Xiao-Long Xu, Xie Yong-tree, Liu Qingliang; Tobacco and fluorescence spectra of CuZnSOD Ⅲ pH value and H_2O_2 sensitivity [J]; Spectroscopy and Spectral Analysis; 2003 05 5 Xiao Rong Hou, Sheng Liangquan, Chun-Hua Shi, Xiao-Long Xu, Yong-tree, Liu Qingliang; salicylic acid and Bovine Serum Albumin by Fluorescence Spectroscopy [J]; Spectroscopy and Spectral Analysis; 2004 01 6 Zhao Changchun, Cheng Wai-fat, Li Mengqiu; berberine and Human Serum Albumin [J]; Spectroscopy analysis; 2004 01 7 Zhou Wenjun, Shen He-Bai, Yang Tao, Yuan joint group; Tb ~ (3) fluorescent ion probe triplex DNA formation [J]; Spectroscopy and Spectral Analysis; 2004 12 8 Wang; Wu Qiuhua ; Wang; Chen Dagang;; quercetin and Bovine Serum Albumin [J]; Spectroscopy and Spectral Analysis; 2006 09 9 Wang; Wuqiu Hua; Wang; Handan Dan; Son Sann home;; Strychnos Base with Bovine Serum Albumin [J]; Spectroscopy and Spectral Analysis; 2007 04 10 YI Ping-Gui, Qing-Sen Yu, Shang Zhi-Cai, Guo Ming; bovine serum albumin binding reaction and the mechanism of aureomycin study [J]; Chemical Physics; 2003 05 Doctoral Dissertation full text database of China before the 4 1 Wang; drugs active ingredient line preconcentration capillary electrophoresis analysis of the interaction between biological macromolecules of [D ]; Hebei Agricultural University; 2007 2 Tangjiang Hong; organic molecules and the interaction of human serum albumin [D]; Lanzhou University; 3, 2006 Fan Xia; methane emissions from cattle manure fertilizer ingredients and fast prediction methods and models of [D]; China Agricultural University; 2004 4 Li Lin Buddha; spectrum of tobacco-based monitoring of the growth and quality of [D]; Nanjing Agricultural University; master's degree in China in 2006 before the full paper 10 1 Liping database; Lycoris species chromosome banding and fluorescence in situ hybridization [D]; Nanjing Forestry University; 2007 2 Wang Huiying; serum albumin and drug molecules interact by Fluorescence [D]; Hebei Normal University; 2004 3 Li Youqin; azo dyes and CD, DNA and protein interactions and its analytical application [D]; Shanxi University; 2006 4 Sheng-Park; new method for the detection of Sudan I and its application [D]; South China University; 2006 more than 5 Lin; DNA-modified gold nanoparticles and their fluorescence and gel electrophoresis [D]; Chongqing University; 6 2006, U Thant; ketones microemulsion fluorescent reagents - Mo (VI) spectra of the probe and application of marker proteins [D ]; Jinan University; 2004 7 Zhang Hui; spectral probe quantitative determination of nucleic acid samples of its mechanism [D]; Jinan University; 2005 8 Dongquan Xi; fluorescence resonance energy transfer in DNA detection of [D ]; Tianjin University; 2007 9 Zhao Junfeng; phosphoryl-dihydroxy-anthraquinone with bovine serum albumin synthesis and the weak interaction [D]; Zhengzhou University; 2007 10 Que Qingmin; several drugs and small molecules Interaction of biological macromolecules [D]; Nanchang University; 2007

Received (12) climb up. Jiang Ming. Mandarin. Zhaoyu Jiang. Wu Fan. Liu different protein to energy ratio of juvenile grass carp feed on digestive enzyme activities [Papers] - Freshwater Fisheries 2009 (6) Chen Ran. Hua Xueming. Huangxu Xiong. Qi Zhou corn gluten meal instead of fish meal on growth of carp, protease activity and apparent digestibility [Papers] - Shanghai Jiaotong University (Agricultural Science) 2009 (4) Dong Xiaohui. Geng Xu. GAVIN school. Huang Xiang Hu. Song Wendong. Wang Hui. tilapia larvae Li Ruiwei Dietary protein levels [Papers] - China Feed 2009 (7) Yang Qihui. ZHOU Qi survival. Zhenghai Juan. Book Review. Dong Xiaohui. Chi Shu Yan cobia organizations of different feeds on digestive enzyme activities [Papers] - Aquatic Sciences 2008 (12) Bai Xiaohui. Xiong Chuanxi different feeds on the fish digestive enzyme activities [Papers] - China Feed 2007 (10) He Jixiang . Dingfeng Qin small peptide and its application in fish nutrition [Papers] - Water Fisheries, 2007 (2) Chen Yong. Qi Zhou. cold to the Army. clock defense of chitosan on carp growth and digestive enzyme [ Papers] - China Sea 2006 (3) Fang Zhanjiang. Blue Fish feeding different view of Hui Tang Comparison of protein content in feed [Papers] - Water Fisheries 2006 (2) Wang Guiqin Culter protein nutritional physiology of [ Dissertation] 2005 Dr. Cai-Hong Hu nanometer copper silicate adsorption of aquatic pathogens, bactericidal activity and its application effect on tilapia and mechanism of [Dissertation] Hui Yu, Dr. 2005. Feng. Liu Donghui. Lianggui Ying cheese protein of small peptides on the growth of young grass carp and feed utilization [Papers] - Aquatic Biology 2004 (5) Wu Jinying after grouper embryo growth and development of lymphoid organs of the digestive system and study [Dissertation] Dr 2004
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About originally gastric pepsin secretion in principal cells, under the conditions in the pH1.5 ~ 5.0, was activated into pepsin, the protein degradation as peptone, and part is broken down into tyrosine, phenylalanine and other amino acids. Determination of gastric juice pepsin can be used to identify the neurological disorder and low-acid low stomach acid disorders, when stomach acid or too little
Absence of pepsin, the pepsin content of the former and the latter is sometimes normal with a lack of hydrochloric acid and pepsin. Low stomach acid is generally believed that disease was due to organic changes in the gastric mucosa caused by severe, especially for pernicious anemia, acid-free patients, no pepsin secretion is an important diagnostic findings. Chronic gastritis, chronic gastric dilatation, chronic enteritis and other twelve fat often reduce the secretion of pepsin. Basal secretion of gastric acid with high general diseases, such as duodenal ulcer, gastric protease activity increased. 1836, Sordo Schwann (TheodorSchwann) in the digestive process of the study, found a substance able to participate in digestion, and named pepsin. Pepsin is the first enzyme obtained from the animals. Stomach only a proteolytic enzyme. The optimum pH value of 1 ~ 2. Pepsin is the main part of the role of aromatic amino acids or amino acid amino acid peptide bond formed. This enzyme is synthesized by the gastric primary cells to secrete zymogen granules in the form, activated by the hydrochloric acid in gastric juice has the ability to digest protein. Medicinal pepsin, can be extracted from the pig stomach, for indigestion. Peptic ulcer disable this drug. Properties White or light yellow powder; no mold smell defeat; have cited moist; aqueous solution was acidic. Identification of the aqueous solution of this product, add tannic acid, gallic acid or the majority of heavy metal salt solution, which precipitate. Check the loss on drying of this product, dried at 100 ℃ for 4 hours, less than 5.0% weight loss may not (Appendix Ⅷ L). Potency Preparation of control solution learn precision that 105 ℃ drying to constant weight tyrosine amount, plus hydrochloric acid 〔take 1mol / L hydrochloric acid 65ml, add water to make 1000ml〕 containing 0.5mg per 1ml of the solution. Basic features of pepsin proteins or peptides in the clipping, with a certain amino acid sequence specificity. For example, it tends to cut N-terminal or C-terminal to aromatic amino acids (such as phenylalanine, tryptophan and tyrosine) or Leu peptide bond; and if the N-terminal peptide bond to a number of third amino acids to basic amino acids (such as lysine, arginine and histidine) or the N-terminal peptide bond of arginine, you can not effectively be cut this peptide bond. The pH value of 1.3 in shear when specific performance is even more obvious: only tend to cut N-terminal
Pepsin Phe or Leu peptide bond. Secreted by the gastric chief cells refers to a molecular weight of 35,000 digestive enzymes. The enzyme is inactive pepsinogen (Pepsinogen) secretion, under the action of hydrochloric acid activation of pepsin. Biodegradable protein phenylalanine or tyrosine and other amino acids from the peptide bond, the product is a small amount of peptone and peptides and amino acids. The optimum pH is around 2. Pepsin in the acidic environment with high activity, the optimum pH value of approximately 3. In neutral or alkaline pH value solution, melting occurs pepsin lost activity. Pepsin activity can be inhibited by pepstatin. First, the activation of the expression of the zymogen of pepsin, which pepsinogen. Pepsin pepsin was originally inactive precursors, the primary structure of pepsin more than 44 amino acids. In the stomach, gastric chief cells release pepsinogen. Acid in the face of the zymogen (released by the parietal cells) in hydrochloric acid after activation. When the stomach to digest food while in a hormone known as gastrin and vagus nerve function, the start of pepsinogen and hydrochloric acid from the stomach in the release. Hydrochloric acid created in the environment, pepsinogen place to fold, making it can be
Pepsin itself from the catalytic approach to the shear, to produce a pepsin activity. Subsequently, the resulting pepsin pepsinogen continue to cut, the 44 amino acid residues Quiché to produce more pepsin. The digestion of food to maintain in the absence of zymogen forms of mechanisms to avoid an excessive amount of pepsin digestion of the stomach wall itself is a protection mechanism. Pepsin action method should be kept at low temperature (-20 ℃ to -80 ℃), in order to prevent their occurrence from degradation. Stored in the solution pH value is greater than 11 or in its reductive methylation can also be effective in preventing the occurrence of self-degradation; when the pH value back to 6, the activity of pepsin can be restored. Stomach digestion is mainly the initial decomposition of protein, pepsin break down proteins with the role, but the principal cells secrete pepsin is inactive zymogen exists, must be based on the role of acid activation and provide the environment, the hydrochloric acid
Gastric pepsin protein zymogen activation, the role of providing the acidic environment of pepsin, is its digestive function. Pepsin secretion originally gastric chief cells, under the conditions in the pH1.5 ~ 5.0, was activated into pepsin, the protein decomposition peptone, and part is broken down into tyrosine, phenylalanine and other amino acids. Test Methods The test tube 6, in which three of the precision reference solution by adding 1ml, the other three joined the precision test solution 1ml, set 37 ℃ ± 0.5 ℃ water bath, heat for 5 minutes, adding preheated to 37 ℃ precision ± 0.5 ℃ hemoglobin test solution 5ml, shake, and accurate time in the 37 ℃ ± 0.5 ℃ water bath for 10 min. Immediately by adding 5% trichloroacetic acid precision solution 5ml, shaking, filtration, the filtrate taken back. In another test tube 2, the precision of hemoglobin test solution by adding 5ml, set 37 ℃ ± 0.5 ℃ water bath for 10 minutes in the moisture,
Pepsin and then adding 5% trichloroacetic acid precision solution 5ml, in which a test solution add 1ml, the other one in the above hydrochloric acid solution 1ml, shaking, filtration, the filtrate obtained, respectively, as the test and reference substance blank control, according to spectrophotometric method (Appendix Ⅳ A) was measured at 275nm wavelength absorbance, calculate the average value of AS and A, calculated as follows. A × Ws × n containing the protease activity per 1g (units) = As × W × 10 × 181.19 AS where the average for the reference substance absorption; A to the test, the average absorption; Ws as the reference solution in each of 1ml with the amount of tyrosine, μg; W is the amount of the test sample, g; n for the dilution of the test. Under these conditions, can catalyze the hydrolysis of hemoglobin per minute generated 1μmol tyrosine enzyme, a protease activity unit. Clinical significance of gastric chief cells originally pepsin secretion in pH1.5 ~ 5.0 conditions, be activated into pepsin, the protein degradation as peptone, and part is broken down into tyrosine, phenylalanine and other amino acids. Determination of gastric juice pepsin can be used to identify the neurological disorder and low-acid low stomach acid disorders, when the acid is too small or lack of, the former is sometimes normal levels of pepsin and hydrochloric acid pepsin and the latter also lacking. Low stomach acid is generally believed that disease was due to organic changes in the gastric mucosa caused by severe, especially for pernicious anemia, acid-free patients, no pepsin secretion is an important diagnostic findings. Chronic gastritis, chronic gastric dilatation, chronic enteritis and other twelve fat often reduce the secretion of pepsin. Basal secretion of gastric acid with high general diseases, such as duodenal ulcer, gastric protease activity by
Pepsin high. Normal: the basis for the secretion of gastric juice pepsin Tyrosine 84.4 ± 9.72mg / h, the maximum amount of pepsin secretion was 190.29 ± 15.31 tyrosine / h (Anson's method); 420 ± 208kU / L (modified Lee's method .) Treatment Product Name: pepsin Pinyin: Weidanbaimei English name: Pepsin This product is a digestive enzyme that the role of gastric acid after the solidification of the protein into and peptone, but not to make further broken down into amino acids. The digestion by 0.2% to 0.4% hydrochloric acid (pH = 1.6 ~ 1.8) when the strongest Guchang combined with diluted hydrochloric acid. Protein for clinical foods because of the oversupply of food digestion, convalescence digestive dysfunction that chronic atrophic gastritis, gastric cancer, pernicious anemia caused by lack of pepsin. Line from pig, sheep or cattle gastric pepsin extracted. Each 1g contains not less than 3,800 units of protease activity. Pepsin deficiency diseases: commonly used in foods because of the oversupply of food protein digestion, convalescence digestive dysfunction, and chronic atrophic gastritis, gastric cancer, pernicious anemia caused by lack of pepsin. Properties: white or light yellow powder; no mold smell defeat; have cited moist; aqueous solution was acidic. Identification: the aqueous solution of this product, add tannic acid, gallic acid or the majority of heavy metal salt solution,
That the precipitation of pepsin. Check: Drying of this product, dried at 100 ℃ for 4 hours, less than 5.0% weight loss may Potency: Precision Preparation of control solution, said drying learn from 105 ℃ to constant weight tyrosine amount, plus hydrochloric acid 〔 take 1mol / L hydrochloric acid 65ml, add water to make 1000ml〕 containing 0.5mg per 1ml of the solution. Preparation of the test solution to take this amount of goods, precision set, made by each of the 1ml of hydrochloric acid solution containing about 0.2 to 0.4 units of solution. Determination of access tube 6, in which three of the precision reference solution by adding 1ml, the other three joined the precision test solution 1ml, set 37 ℃ ± 0.5 ℃ water bath, heat for 5 minutes, adding preheated to 37 ℃ precision ± 0.5 ℃ hemoglobin test solution 5ml, shake, and accurate time in the 37 ℃ ± 0.5 ℃ water bath for 10 min. Immediately by adding 5% trichloroacetic acid precision solution 5ml, shaking, filtration, the filtrate taken back. In another test tube 2, the precision of hemoglobin test solution by adding 5ml, set 37 ℃ ± 0.5 ℃ water bath for 10 minutes in the moisture, then precision of 5% trichloroacetic acid solution by adding 5ml, in which a test solution add 1ml, the other one Add the hydrochloric acid solution 1ml, shaking, filtration, the filtrate obtained, respectively, as the test and reference substances control, according to the wavelength spectrophotometry was measured at 275nm absorbance, calculate the average value of AS and A, press calculated. A × Ws × n containing the protease activity per 1g (units) = As × W × 10 × 181.19 AS where the average for the reference substance absorption; A to the test, the average absorption; Ws as the reference solution in each of 1ml with the amount of tyrosine, μg; W is the amount of the test sample, g; n for the dilution of the test. Under these conditions, can catalyze the hydrolysis of hemoglobin per minute generated 1μmol tyrosine enzyme, a protease activity unit. Category: Zhuxiaohuayao. Storage: sealed in a dry place. Preparations: (1) pepsin tablets (2) pepsin particles (3) sugar stomach pepsin digest food experts suggest the role of the stomach to secrete gastric juice is, gastric juice pepsin, hydrochloric acid can activate the element, make it pepsin, and pepsin can digest the protein in food. Cattle into the human gastric stomach after being eaten, it contains protein, the stomach produces digestive juice was gradually digested. The stomach to digest meat, but its own safe. To this end, the Department of Medicine, University of Michigan professor of Durban did an interesting experiment. He cut the body down from the stomach into a large test tube, then add the appropriate amount of normal human stomach, according to the concentration of hydrochloric acid and pepsin preparation, the tube placed in the 37 ℃ constant temperature environment. Result, the stomach tube was seriously damaged, and a considerable portion was dissolved out. This experiment shows that the stomach could not withstand the hydrochloric acid and pepsin digestion. Professor Durban
Further studies have shown that pepsin, the stomach can be damaged, but can easily be repaired, it is this mechanism to implement the important function of protecting the surface of the stomach. He pointed out that the parietal cells of the cell membrane lipids, and has a lot to resist digestion, if the cell surface with detergent to remove lipids, acid gastric parietal cells would be violated. In addition, the parietal cells frequently updated, the old cells are constantly shed from the surface by new cells within the organization instead. Germany and the professor, estimates that the human stomach about 500,000 per minute, cell loss, mucosal layer of all the updates every 3 days once. So, even if the inner wall of the stomach against a certain extent, can also be fully restored within a few days or hours. So the body does not digest the stomach itself is not, but is digested to some degree immediately after the self-renewal. After years of research and some scientists have confirmed the formation of gastric ulcer gastric local organizations are gastric acid and pepsin digestion of the results; this self-digestion process is the direct cause of ulcer formation; gastric digestion is an important factor in the formation of ulcers one. Biochemistry pharmaceutical manufacturer Qingdao, Shandong, Guangdong Jiangmen Universal Pharmaceutical Co., Ltd., Shaanxi Central America Pharmaceutical, Chongqing Pharmaceutical Factory Riverside, Chongqing mountains meet pharmaceutical, biochemical pharmaceutical factory in Liuzhou, Guilin, Li River Pharmaceuticals Co., Ltd., Chengdu Tong Tak Pharmaceutical Co., Ltd., Mianyang City, biochemistry laboratories, Neijiang Biochemical Pharmaceutical Co., Ltd. Long March, Kaifeng biochemistry laboratories, pharmaceutical companies have the spring in Luoyang, Nanchang biochemical pharmaceutical factory, Zhejiang the beginning of the peak roof pharmaceutical Province, east Sichuan Pharmaceutical Co., Ltd., Chengdu and biochemical laboratories, pharmaceutical Guangyuan, Sichuan Province, Xi'an biological laboratories, pharmaceutical biochemistry Pingliang, Gansu Longxi biochemical system pharmaceutical, biological agent factories in Kunming, Zhejiang Huangyan biochemistry laboratories, pharmaceutical biochemistry, Weifang, Shandong, Shandong Laiyang biochemical pharmaceutical Co., Ltd. Shandong intellectual panacea, Chinachem Shuanghui (Group), Henan Shangqiu area biochemistry laboratories, Hengyang Fu Pharmaceutical Co., Ltd., Texas Health and of medicine and health products company, the Shanghai Biochemical Pharmaceutical Factory Great Wall, Tianjin Second biochemical laboratories, pharmaceutical biochemistry, Yangquan, Shanxi, Hill
Pepsin West Province biochemical pharmaceutical factory in Changzhi City, Shanxi Linfen Biochemical Pharmaceutical Factory, Dalian Biochemical Pharmaceutical Factory, Mudanjiang City biochemistry laboratories, biochemical pharmaceutical factory in Shenyang, Changchun, Chongqing Mayor Biochemical Pharmaceutical Factory, Taiyuan biochemistry laboratories, pharmaceutical factory in Baoding Biochemistry.