Immunoadsorbent affinity purification of the two enzyme forms of α‐mannosidase from Phaseolus vulgaris
1976; Wiley; Volume: 72; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(76)80808-3
ISSN1873-3468
Autores Tópico(s)Enzyme Production and Characterization
ResumoFEBS LettersVolume 72, Issue 1 p. 39-42 Full-length articleFree Access Immunoadsorbent affinity purification of the two enzyme forms of α-mannosidase from Phaseolus vulgaris Elisabeth Paus, Elisabeth Paus Anatomical Institute, University of Oslo, Karl Johansgt. 47, Oslo 1, NorwaySearch for more papers by this author Elisabeth Paus, Elisabeth Paus Anatomical Institute, University of Oslo, Karl Johansgt. 47, Oslo 1, NorwaySearch for more papers by this author First published: December 15, 1976 https://doi.org/10.1016/0014-5793(76)80808-3Citations: 10AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 T.-Y. Li, J. Biol. Chem., 242, (1967), 5474– 5480. 2 E. Paus, T.B. Christensen, Eur. J. Biochem., 25, (1972), 308– 314. 3 K.M.L. Agrawal, O.P. Bahl, J. Biol. Chem., 243, (1968), 103– 111. 4 S. Snaith, G.A. Levvy, Biochem. J., 114, (1969), 25– 33. 5 S. Snaith, Biochem. J., 147, (1975), 83– 90. 6 G.H. Jones, C.E. Bahlou, J. Biol. Chem., 244, (1969), 1043– 1051. 7 J. Conchie, J. Findlay, G.A. Levvy, Biochem J., 71, (1959), 318– 325. 8 T. Okumura, I. Yamashina, J. Biochem. (Tokyo), 73, (1973), 131– 138. 9 J. Conchie, A.J. Hay, Biochem. J., 87, (1963), 354– 361. 10 C.A. Marsh, G.C. Gourlay, Biochim. Biophys. Acta, 235, (1971), 142– 148. 11 M. Chester, A. Lundblad, K.M. Parvesh, Biochim. Biophys. Acta, 391, (1975), 341– 348. 12 M. Carroll, N. Dance, P.K. Massou, D. Robinson, B.G. Winchester, Biochem. Biophys. Res. Commun., 49, (1972), 579– 583. 13 N.C. Phillips, D. Robinson, B.G. Winchester, R.D. Jolly, Biochem. J., 137, (1974), 363– 371. 14 N.E. Nordén, A. Lundblad, P.A. Öckerman, R.D. Jolly, FEBS Lett., 35, (1973), 209– 212. 15 O.H. Lowry, N.J. Roseborough, A.L. Farr, R.J. Randall, J. Biol. Chem., 193, (1951), 265– 275. 16 M. Harboe, A. Ingild, Scand. J. Immunol., 2, (1973), 161– 164. Suppl. 1 17 J. Porath, R. Axén, S. Ernback, Nature (London), 215, (1967), 1491– 1492. 18 T. Eskeland, E. Klein, M. Inoue, B. Johansson, J. ExP. Med., 134, (1971), 265– 280. 19 J.J. Scheidegger, Int. Arch. Allergy, 7, (1955), 103– 110. 20 B.J. Davis, Ann. N.Y. Acad. Sci., 121, (1964), 404– 427. Citing Literature Volume72, Issue1December 15, 1976Pages 39-42 ReferencesRelatedInformation
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