Application of the proteolytic enzyme papain in routine platelet serology
By:
J.A.G. Lown and B.J. Dale
Paid access
|Nov 2020References
- Mollison PL, Engelfreit CP, Contreas M. Blood transfusion in clinical medicine. 8th ed. London: Blackwell, 1987:457–8.
- McGowan EB, Yeo KT, Detwiler TC. The action of calcium dependent protease on platelet surface glycoproteins. Arch Biochem Biophys 1983;227:287–301.<dgdoi:pub-id xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" pub-id-type="doi"><a href="https://doi.org/10.1016/0003-9861(83)90373-9" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">10.1016/0003-9861(83)90373-9</a></dgdoi:pub-id>
- Take H, Tomiyama Y, Shibata Y, et al. Demonstration of the heterogeneity of epitopes of the platelet specific alloantigen, Bak<sup>a</sup>. Br J Haematol 1990;76:395–400.<dgdoi:pub-id xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" pub-id-type="doi"><a href="https://doi.org/10.1111/j.1365-2141.1990.tb06374.x" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">10.1111/j.1365-2141.1990.tb06374.x</a></dgdoi:pub-id>
- Lown JAG, Ivey JG. Evaluation of a solid phase red cell adherence technique for platelet antibody screening. Transfus Med 1991;1:163–7.<dgdoi:pub-id xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" pub-id-type="doi"><a href="https://doi.org/10.1111/j.1365-3148.1991.tb00026.x" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">10.1111/j.1365-3148.1991.tb00026.x</a></dgdoi:pub-id>
- Horsewood P, Smith JW, Kelton HG. Monoclonal antibodies against platelet glycoproteins. Transfus Med Rev 1993;7:156–72.<dgdoi:pub-id xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" pub-id-type="doi"><a href="https://doi.org/10.1016/S0887-7963(93)70135-2" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">10.1016/S0887-7963(93)70135-2</a></dgdoi:pub-id>
- Luner SJ, Sturgeon P, Azlarek D, McQuiston DT. Effects of proteases and neuraminidase on red cell surface charge and agglutination: a kinetic study. Vox Sang 1975;28:184–99.<dgdoi:pub-id xmlns:dgdoi="http://degruyter.com/resources/doi-from-crossref" pub-id-type="doi"><a href="https://doi.org/10.1111/j.1423-0410.1975.tb02757.x" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">10.1111/j.1423-0410.1975.tb02757.x</a></dgdoi:pub-id><dgpm:pub-id xmlns:dgpm="http://degruyter.com/resources/fetched-pubmed-id" pub-id-type="pmid">164087</dgpm:pub-id>
DOI: https://doi.org/10.21307/immunohematology-2019-805 | Journal eISSN: 1930-3955 | Journal ISSN: 0894-203X
Language: English
Page range: 140 - 142
Published on: Nov 17, 2020
Published by: American National Red Cross
In partnership with: Paradigm Publishing Services
Publication frequency: 4 times per year
Related subjects:
© 2020 J.A.G. Lown, B.J. Dale, published by American National Red Cross
This work is licensed under the Creative Commons License.