The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
The Neutral Proteases of Human Granulocytes: Isolation and Partial Characterization of Granulocyte Elastases
Open accessAbstract
Elastolytic enzymes were isolated from the extract of the lysosome‐like granules of human leukaemic myeloid cells by chromatography on Sephadex G‐75, ɛAhx‐Sepharose 4 B, elastin‐Sepharose 4 B and preparative agarose‐gel electrophoresis. The elastase were cationic proteins but appeared as three proteins with a slight difference in electrophoretic mobility. The three elastases degraded native, insoluble elastin with a pH optimum of about 8.5. The granulocyte elastases were inactivated by α 1‐antitrypsin and α 2‐macroglobin. The amino‐acid composition of the three elastases was the same except for a variation in arginine content. Dodecylsulfate‐electrophoresis suggested molecular weights in the range 33000–36000. The s20, w0 value determined for one of the elastases was 2.6 S. The three elastases gave the reaction of identity on immunodiffusion according to Ouchterlony and crossed immunoelectrophoresis. They showed the same type of reaction with elastase partly purified from normal human granulocytes, which also contained three separate elastolytic enzymes.
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Metadata
- Authors
- Ohlsson, K., & Odsson, I.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1974-03
- Volume
- 42
- Issue
- 2
- Pages
- 519-527
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1862138102
- Cited by
- 311
- References
- 14
- FWCI
- 15.99
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ohlsson, K., & Odsson, I. (1974). The Neutral Proteases of Human Granulocytes: Isolation and Partial Characterization of Granulocyte Elastases. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1974.tb03367.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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