[Fractures of the coxal femur end. Development of surgical treatment and rehabilitation (1973-1978)]. / Frakturen am koxalen Femurende. Entwicklung der operativen Versorgung und Rehabilitation (1973 bis 1978).

734 fractures of the proximal femur end treated between 1973 and 1978 are presented in order to demonstrate the progress of surgical treatment and rehabilitation as well as the advantages of certain methods.

The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (position 1--222).

The amino terminal 227 amino acid residues of the alpha 1(III) chain contain four CNBr peptides: alpha 1(III)CB3A (79 residues), CB3B, CB3C (6 residues each), CB7 (37 residues) and CB6 (99 residues). Fragmentation of the CNBr peptides was carried out using trypsin, chymotrypsin and the protease from Staphylococcus aureus V8. The fragments obtained were isolated by a combination of molecular sieve and ion exchange chromatography. The sequence analysis was performed according to the automated Edman degradation procedure.

The covalent structure of calf skin type III collagen. VI. The amino acid sequence of the carboxyterminal cyanogen bromide peptide alpha 1(III)CB9B (position 928--1028).

The C-terminal cyanogen bromide peptide alpha 1(III)CB9B is 101 amino acid residues in length and occupies position 928--1028 along the alpha 1(III) chain. For sequence analysis, alpha 1(III)CB9B was fragmented with trypsin and chymotrypsin. The peptides obtained were separated using molecular sieve and ion exchange chromatography and sequenced using the automated Edman degradation procedure.

Ordering of cyanogen bromide peptides of type III collagen based on their homology to type I collagen: preservation of sites for crosslink formation during evolution.

The order of the cyanogen-bromide-derived peptides from alpha 1 (III) chains of pepsin-solubilized calf skin collagen was found to be 3A-3B-3C-7-6-1,8,2-4-5-9A-9B. The amino-acid sequences of the NH2-terminal region of all peptides were determined by Edman's automated degradation procedure. The alignment of the peptides along the peptide chain was established by searching for the best homology between the partial sequences of the cyanogen bromide peptides from the alpha 1 (III) chain and the completely known sequence of the alpha 1 (I) chain. Characterization of three cyanogen-bromide-derived double peptides provided confirmation of the deduced order. A sequence Gly-Met-Hyl-Gly-His-Arg-Gly-Phe- was established near the NH2-terminus and a sequence Gly-Ile-Hyl-Gly-His-Arg-Gly-Phe near the COOH-terminus of the alpha 1(III) chain. Identical sequences have been found in the corresponding regions of the alph 1(I) chain. They include hydroxylysine, a site for intermolecular crosslink formation. Because these sequences are conserved during evolution of the collagen molecule, they are probably important for collagen structure and function.

Isolation and characterization of CNBr derived peptides of the alpha1 (III) chain of pepsin-solubilized calf skin collagen.

Fetal calf skin was solubilized by limited pepsin digestion and type III collagen separated from type I collagen by fractional salt precipitations. Cleavage of the type III collagen with CNBr gave rise to ten peptides, which were isolated by molecular sieve and ion exchange chromatography. The peptides were characterized by determination of their molecular weights and amino acid compositions. Together they account for all the amino acids and total molecular weight of the alpha1 (III) chain. Six of the peptides contain more hydroxyproline than proline residues. The two cysteinyl residues of the alpha1 (III) chain which provide sites for interchain disulfide bonding were localized in the C-terminal CNBr peptide. In addition to the ten CNBr peptides, three double peptides were isolated which still contained one methionine residue. About 0.1 residue Gal-Hyl monosaccharide and 0.8 Glc-Gal-Hyl residue disaccharide were found per alpha1 (III) chain. Almost all hydroxylysine-bound carbohydrate was located on peptide 7.