The DOI matches its Crossref record.
The nature of the link between protein and carbohydrate of a chondroitin sulphate complex from hyaline cartilage
Open accessAbstract
TRANSAMINASES OF WHEAT GERM 195 2. The glutamic-alanine transaJninase has an equilibrium constant of 1-4 at 250 and pH 7 5, and an optimum pH of 7*5.3. The glutamic-aspartic enzyme has an equilibrium constant of 5 0 at 250 and pH 8 and an optimum pH between pH 8-0 and 8-5.4. The effect of pyridoxal phosphate and some inhibitors on the transaminases suggests that the two systems may be catalysed by two different enzymes, as are the animal glutamic-alanine and glutamic-aspartic transarninase systems.
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Cited by
A note on the determination of the ester sulphate content of sulphated polysaccharides
DODGSON, K., & PRICE, R. (1962) · Biochemical Journal · doi:10.1042/bj0840106 · Cited by 1,645
Hill, R. L. (1965) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60388-5 · Cited by 411
A personal voyage through the proteoglycan field
Lindahl, U. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.001 · Cited by 28
Metadata
- Authors
- Muir, H.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1958-06-01
- Volume
- 69
- Issue
- 2
- Pages
- 195-204
- ISSN
- 0306-3283 (ISSN-L)
- OpenAlex
- W1850737177
- Cited by
- 278
- References
- 0
- FWCI
- 7.62
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Muir, H. (1958). The nature of the link between protein and carbohydrate of a chondroitin sulphate complex from hyaline cartilage. Biochemical Journal. https://doi.org/10.1042/bj0690195
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
