Abstract
1. The interaction of acid mucopolysaccharides of connective tissue with solubilized collagen of native, or near-native, structure was investigated by free solution electrophoresis at pH7·0. 2. Complex-formation was detected by the appearance of a third peak in the ascending limb only, indicating reversible association. 3. Complex-formation was destroyed by prior heating of solubilized collagen, indicating a probable requirement for high molecular weight or internal structure of the protein. 4. Hyaluronate and chondroitin sulphate of mol.wt. 50000 gave complexes with soluble collagen at I 0·4, whereas heparin and chondroitin sulphate of mol.wt. 15000–18000 did not. All mucopolysaccharides yielded complexes at I 0·1. The stability of the complex appears mainly dependent on electrostatic forces and is increased with increase in chain length of the polysaccharide. 5. Solubilized collagen interacted to yield gels with the `native' chondroitin sulphate–protein macro-molecule from cartilage. 6. A schematic model for the interaction of collagen and chondroitin sulphate–protein macromolecules shows parallel-ordered interaction of collagen fibrils with chondroitin sulphate side chains of the chondroitin sulphate–protein macromolecule. The biological implications of this model are discussed, particularly in relation to the ordered structures and the ionic-network properties of the intercellular components of connective tissue.
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- ANDERSON A. J., LACK C. H. THE FORMATION, COMPOSITION AND FIBRINOLYTIC POTENTIAL OF CHONDROMUCOPROTEIN-FIBRINOGEN AND CHONDROMUCOPROTEIN-LIPOPROTEIN COMPLEXES IN HUMAN EUGLOBULIN FRACTIONS. Clin Sci. 1964 Feb;26:97–110. [PubMed] [Google Scholar]
- ANDERSON A. J. THE FORMATION OF CHONDROMUCOPROTEIN-FIBRINOGEN AND CHONDROMUCOPROTEIN-BETA-LIPOPROTEIN COMPLEXES. Biochem J. 1963 Sep;88:460–469. doi: 10.1042/bj0880460. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BADIN J., SCHUBERT M. Conditions of formation of euglobulin-like precipitates from serum proteins and chondroitin sulfate. J Clin Invest. 1955 Aug;34(8):1312–1316. doi: 10.1172/JCI103177. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BANGA I., BALO J. Isolation of neutral heteropolysaccharide containing mucoprotein from bovine Achilles tendon with the aid of collagenmucoproteinase. Biochem J. 1960 Feb;74:388–393. doi: 10.1042/bj0740388. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BERNFELD P., DONAHUE V. M., BERKOWITZ M. E. Interaction of human serum beta-lipoglobulin with polyanions. J Biol Chem. 1957 May;226(1):51–64. [PubMed] [Google Scholar]
- DAVIES M., NICHOL L. W., OGSTON A. G. FRICTIONAL EFFECTS IN THE MIGRATION OF MIXTURES OF HYALURONIC ACID AND SERUM ALBUMIN. Biochim Biophys Acta. 1963 Nov 29;75:436–438. doi: 10.1016/0006-3002(63)90631-0. [DOI] [PubMed] [Google Scholar]
- DORFMAN A. METABOLISM OF ACID MUCOPOLYSACCHARIDES. Biophys J. 1964 Jan;4:SUPPL155–SUPPL165. doi: 10.1016/s0006-3495(64)86935-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
- EINBINDER J., SCHUBERT M. Binding of mucopolysaccharides and dyes by collagen. J Biol Chem. 1951 Jan;188(1):335–341. [PubMed] [Google Scholar]
- ELDEN H. R. HYDRATION OF CONNECTIVE TISSUE AND TENDON ELASTICITY. Biochim Biophys Acta. 1964 May 25;79:592–599. doi: 10.1016/0926-6577(64)90225-6. [DOI] [PubMed] [Google Scholar]
- FESSLER J. H. A structural function of mucopolysaccharide in connective tissue. Biochem J. 1960 Jul;76:124–132. doi: 10.1042/bj0760124. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GRAMLING E., NIEDERMEIER W., HOLLEY H. L., WARD P. Some factors affecting the interaction of hyaluronic acid with bovine-plasma albumin. Biochim Biophys Acta. 1963 Mar 5;69:552–558. doi: 10.1016/0006-3002(63)91307-6. [DOI] [PubMed] [Google Scholar]
- HARTMANN F. [The nature of functional disorders of connective tissue]. Verh Dtsch Ges Inn Med. 1959;65:27–53. [PubMed] [Google Scholar]
- HEDBLOM E. E. The role of polysaccharides in corneal swelling. Exp Eye Res. 1961 Sep;1:81–91. doi: 10.1016/s0014-4835(61)80012-2. [DOI] [PubMed] [Google Scholar]
- Hodge A. J., Schmitt F. O. THE CHARGE PROFILE OF THE TROPOCOLLAGEN MACROMOLECULE AND THE PACKING ARRANGEMENT IN NATIVE-TYPE COLLAGEN FIBRILS. Proc Natl Acad Sci U S A. 1960 Feb;46(2):186–197. doi: 10.1073/pnas.46.2.186. [DOI] [PMC free article] [PubMed] [Google Scholar]
- JACKSON D. S. The nature of collagen-chondroitin sulphate linkages in tendon. Biochem J. 1954 Apr;56(4):699–703. doi: 10.1042/bj0560699. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KEECH M. K. The formation of fibrils from collagen solutions. IV. Effect of mucopolysaccharides and nucleic acids: an electron microscope study. J Biophys Biochem Cytol. 1961 Jan;9:193–209. doi: 10.1083/jcb.9.1.193. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LAURENT T. C. Studies on fractionated heparin. Arch Biochem Biophys. 1961 Feb;92:224–231. doi: 10.1016/0003-9861(61)90341-1. [DOI] [PubMed] [Google Scholar]
- LOEVEN W. A. The complex binding between protein and mucopolysaccharide in connective tissue. Acta Physiol Pharmacol Neerl. 1956 Dec;5(2):121–146. [PubMed] [Google Scholar]
- MATHEWS M. B., LOZAITYTE I. Sodium chondroitin sulfate-protein complexes of cartilage. I. Molecular weight and shape. Arch Biochem Biophys. 1958 Mar;74(1):158–174. doi: 10.1016/0003-9861(58)90210-8. [DOI] [PubMed] [Google Scholar]
- MATHEWS M. B. Sodium condroitin sulfate-protein complexes of cartilage. III. Preparation from shark. Biochim Biophys Acta. 1962 Mar 26;58:92–101. doi: 10.1016/0006-3002(62)90821-1. [DOI] [PubMed] [Google Scholar]
- MATHEWS M. B. The molecular weight of sodium chondroitin sulfate by light scattering. Arch Biochem Biophys. 1956 Apr;61(2):367–377. doi: 10.1016/0003-9861(56)90359-9. [DOI] [PubMed] [Google Scholar]
- NEMETH-CSOKA M. [Studies of collagen fibers. Part 1. On the submicroscopic structure of collagen fibers prepared in vitro and the stabilizing role of acid mucopolysaccharides]. Acta Histochem. 1960 Jun 30;9:282–294. [PubMed] [Google Scholar]
- NEMETH-CSOKA M. [Studies on collagen fibers. II. Comparative chemical, polarization and electron microscopic studies on collagen fibers with chondroitin sulfate as the basic substance]. Acta Histochem. 1961 Dec 30;12:255–276. [PubMed] [Google Scholar]
- OFFRET G., PAYRAUP, POULIQUENY, FAURE J. P., HAMEAU J. P. [The mucopolysaccharides of the cornea: distribution, role, changes in normal and pathological corneas]. Arch Ophtalmol Rev Gen Ophtalmol. 1962 Oct-Nov;22:699–722. [PubMed] [Google Scholar]
- PARTINGTON F. R., WOOD G. C. The role of non-collagen components in the mechanical behaviour of tendon fibres. Biochim Biophys Acta. 1963 Mar 5;69:485–495. doi: 10.1016/0006-3002(63)91298-8. [DOI] [PubMed] [Google Scholar]
- PIGMAN W., GRAMLING E., HOLLEY H. L. Interactions of hyaluronic acid with serum albumin. Biochim Biophys Acta. 1961 Jan 1;46:100–107. doi: 10.1016/0006-3002(61)90651-5. [DOI] [PubMed] [Google Scholar]
- Partridge S. M. The chemistry of connective tissues. 1. The state of combination of chondroitin sulphate in cartilage. Biochem J. 1948;43(3):387–397. [PMC free article] [PubMed] [Google Scholar]
- ROGERS H. J. The structure and function of hyaluronate. Biochem Soc Symp. 1961;20:51–79. [PubMed] [Google Scholar]
- SYLVEN B., AMBROSE E. J. Birefingent fibres of hyaluronic acid. Biochim Biophys Acta. 1955 Dec;18(4):587–587. doi: 10.1016/0006-3002(55)90164-5. [DOI] [PubMed] [Google Scholar]
- THOMAS L. THE EFFECTS OF PAPAIN, VITAMIN A, AND CORTISONE ON CARTILAGE MATRIX IN VIVO. Biophys J. 1964 Jan;4:SUPPL207–SUPPL213. doi: 10.1016/s0006-3495(64)86939-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- THOMPSON T. E., McKERNAN W. M. An electrophoretic investigation of interactions between bovine plasma albumin and charged dextran derivatives. Biochem J. 1961 Oct;81:12–23. doi: 10.1042/bj0810012. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WOOD G. C. The formation of fibrils from collagen solutions. 3. Effect of chondroitin sulphate and some other naturally occurring polyanions on the rate of formation. Biochem J. 1960 Jun;75:605–612. doi: 10.1042/bj0750605. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WOODIN A. M., BORUCHOFF S. A. Particle interaction in solutions derived from ox vitreous humor. J Biophys Biochem Cytol. 1955 Nov 25;1(6):489–500. doi: 10.1083/jcb.1.6.489. [DOI] [PMC free article] [PubMed] [Google Scholar]


