{"title":"青霉菌的蛋白水解酶。一种胰蛋白酶原活化酶(肽酶a)的纯化和性质。","authors":"T. Hofmann , R. Shaw","doi":"10.1016/0926-6569(64)90014-8","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>(1) A trypsinogen-activating proteolytic enzyme (peptidase A) has been isolated from the growth medium of <em>Penicillium janthinellum</em> and purified about 60-fold; it is homogeneous in the ultra-centrifuge and on electrophoresis. Its molecular weight is 32 000.</p></span></li><li><span>2.</span><span><p>(2) The enzyme has the following amino acid composition: Lys<sub>5</sub>, His<sub>3</sub>, Asp<sub>36</sub>, Thr<sub>28</sub>, Ser<sub>42</sub>, Glu<sub>28</sub>, Pro<sub>12</sub>, Gly<sub>39</sub>, Ala<sub>23</sub>, Val<sub>22</sub>, Ileu<sub>12.5</sub>, Leu<sub>20</sub>, Tyr<sub>14</sub>, Phe<sub>19</sub>, Try<sub>4–5</sub>. It does not contain arginine, methione and half-crystine.</p></span></li><li><span>3.</span><span><p>(3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving <em>K</em><sub>m</sub> = (7.6±2) · 10<sup>−6</sup> M (at 0°, pH 3.4).</p></span></li><li><span>4.</span><span><p>(4) Peptidase A apparently does not act on small peptides, but readily degrades apoferritin and bovine serum albumin. About 15% of the peptide bonds in bovine serum albumin are hydrolysed.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 543-557"},"PeriodicalIF":0.0000,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90014-8","citationCount":"47","resultStr":"{\"title\":\"Proteolytic enzymes of Penicillium janthinellum\",\"authors\":\"T. Hofmann , R. Shaw\",\"doi\":\"10.1016/0926-6569(64)90014-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>(1) A trypsinogen-activating proteolytic enzyme (peptidase A) has been isolated from the growth medium of <em>Penicillium janthinellum</em> and purified about 60-fold; it is homogeneous in the ultra-centrifuge and on electrophoresis. Its molecular weight is 32 000.</p></span></li><li><span>2.</span><span><p>(2) The enzyme has the following amino acid composition: Lys<sub>5</sub>, His<sub>3</sub>, Asp<sub>36</sub>, Thr<sub>28</sub>, Ser<sub>42</sub>, Glu<sub>28</sub>, Pro<sub>12</sub>, Gly<sub>39</sub>, Ala<sub>23</sub>, Val<sub>22</sub>, Ileu<sub>12.5</sub>, Leu<sub>20</sub>, Tyr<sub>14</sub>, Phe<sub>19</sub>, Try<sub>4–5</sub>. It does not contain arginine, methione and half-crystine.</p></span></li><li><span>3.</span><span><p>(3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving <em>K</em><sub>m</sub> = (7.6±2) · 10<sup>−6</sup> M (at 0°, pH 3.4).</p></span></li><li><span>4.</span><span><p>(4) Peptidase A apparently does not act on small peptides, but readily degrades apoferritin and bovine serum albumin. About 15% of the peptide bonds in bovine serum albumin are hydrolysed.</p></span></li></ul></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 3\",\"pages\":\"Pages 543-557\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-12-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90014-8\",\"citationCount\":\"47\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964900148\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964900148","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
(1) A trypsinogen-activating proteolytic enzyme (peptidase A) has been isolated from the growth medium of Penicillium janthinellum and purified about 60-fold; it is homogeneous in the ultra-centrifuge and on electrophoresis. Its molecular weight is 32 000.
2.
(2) The enzyme has the following amino acid composition: Lys5, His3, Asp36, Thr28, Ser42, Glu28, Pro12, Gly39, Ala23, Val22, Ileu12.5, Leu20, Tyr14, Phe19, Try4–5. It does not contain arginine, methione and half-crystine.
3.
(3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving Km = (7.6±2) · 10−6 M (at 0°, pH 3.4).
4.
(4) Peptidase A apparently does not act on small peptides, but readily degrades apoferritin and bovine serum albumin. About 15% of the peptide bonds in bovine serum albumin are hydrolysed.