Self-aggregation of squid cranial cartilage proteoglycans
(1992) In Matrix (Stuttgart, Germany) 12(6). p.417-426- Abstract
- Squid cranial cartilage has been found to contain three different proteoglycan populations, two of which form aggregates (Vynios, D.H. and Tsiganos, C. P., Biochim. Biophys. Acta 1033: 139-147, 1990). The aggregation involves interaction of their protein cores as assessed by electron microscopy and biochemical data. Aggregating oligopeptides were isolated after mild trypsin digestion which inhibited self-aggregation of proteoglycans. The aggregation does not involve interaction of the side chains of polar amino acids and evidence is provided that it is mediated through hydrophobic interaction. It is enhanced upon concentration or incubation of the samples at 37 degrees C.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1106688
- author
- Vynios, D H ; Mörgelin, Matthias LU and Tsiganos, C P
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Matrix (Stuttgart, Germany)
- volume
- 12
- issue
- 6
- pages
- 417 - 426
- publisher
- Elsevier
- external identifiers
-
- pmid:1287410
- scopus:0027064937
- ISSN
- 0934-8832
- language
- English
- LU publication?
- yes
- id
- cd1109ae-b7f7-4733-93d1-b146b98ea222 (old id 1106688)
- date added to LUP
- 2016-04-01 15:27:37
- date last changed
- 2021-01-03 06:17:46
@article{cd1109ae-b7f7-4733-93d1-b146b98ea222, abstract = {{Squid cranial cartilage has been found to contain three different proteoglycan populations, two of which form aggregates (Vynios, D.H. and Tsiganos, C. P., Biochim. Biophys. Acta 1033: 139-147, 1990). The aggregation involves interaction of their protein cores as assessed by electron microscopy and biochemical data. Aggregating oligopeptides were isolated after mild trypsin digestion which inhibited self-aggregation of proteoglycans. The aggregation does not involve interaction of the side chains of polar amino acids and evidence is provided that it is mediated through hydrophobic interaction. It is enhanced upon concentration or incubation of the samples at 37 degrees C.}}, author = {{Vynios, D H and Mörgelin, Matthias and Tsiganos, C P}}, issn = {{0934-8832}}, language = {{eng}}, number = {{6}}, pages = {{417--426}}, publisher = {{Elsevier}}, series = {{Matrix (Stuttgart, Germany)}}, title = {{Self-aggregation of squid cranial cartilage proteoglycans}}, volume = {{12}}, year = {{1992}}, }