Variation in quantity and extractability of the 148-kilodalton cartilage protein with age.

The occurrence of non-collagenous matrix proteins was studied in samples of tracheal cartilage from steers of different ages. The amounts of the 148 kDa cartilage protein in 4M-guanidinium chloride extracts and in subsequent trypsin digests of the extraction residues were determined by radioimmunoassay. Surprisingly, the 148 kDa-protein antigenicity was not changed by tryptic digestion, even though the protein was extensively degraded. The amount of the 148 kDa protein increased dramatically with age, both in the guanidinium chloride extract and in the subsequent tryptic digest, and reached maximal values at about 3 and 8 years respectively. The increase of the guanidinium chloride-soluble pool preceded that of the trypsin-digestible pool, possibly indicating a metabolic relationship. The ratio between the trypsin-digestible and guanidinium chloride-soluble pools increased continuously, and at 12 years of age close to 90% of the total 148 kDa protein detected was insoluble in guanidinium chloride. At all ages, the bulk of the cartilage collagen was insoluble both to extraction with guanidinium chloride and to tryptic digestion. The decreasing extractability of the 148 kDa protein was therefore not secondary to changes in the solubility of the collagen network. Other cartilage proteins, such as the link proteins and the 36 kDa protein, showed much smaller quantitative variations of a different character.     

Calliandra (Leguminosae) in continental Africa

The mainly neotropical genus Calliandra Benth. (Leguminosae–Mimosoideae–Ingeae) is reported for the first time as native in continental Africa. There are two species known, C. gilbertii Thulin & Hunde sp. nov. in E Kenya and Somalia and C. redacta (J. H. Ross) Thulin & Hunde comb. nov. in South Africa near the Namibia border. On pollen morphological grounds they are supposed to be most related to certain neotropical species but the pollen does not agree entirely with any previously known group of the genus. The distribution of C gilbertii and C. redacta stresses the phytogeographical link between the arid zones of northern and southern Africa.     

Cartilage matrix proteins. A basic 36-kDa protein with a restricted distribution to cartilage and bone

A non-collagenous quantitatively prominent protein was purified from guanidine hydrochloride extracts of bovine tracheal cartilage. Purification was achieved by cesium chloride density gradient centrifugation and chromatography on DEAE-cellulose at pH 7.0 followed by CM-cellulose at pH 5.0. The protein has a marked tendency to form aggregates in denaturing solutions of high ionic strength, e.g. 6 M guanidine hydrochloride. The purified protein contains a single, Mr 36,000 polypeptide chain, with a particularly high content of leucine. It contains about 1% carbohydrate with a remarkable absence of hexosamines and sialic acid, whereas xylose, galactose, mannose, and fucose were identified in the preparation. The protein was identified in extracts of cartilage and bone and could be shown to be primarily extracellular. Tendon may contain trace amounts of the protein, whereas extracts of several other tissues showed no immunoreactivity in enzyme-linked immunosorbent assay.     

An abundant chick gizzard integrin is the avian alpha 1 beta 1 integrin heterodimer and functions as a divalent cation-dependent collagen IV receptor.

The alpha-subunit of an abundant chick gizzard integrin was isolated (T. Kelly, L. Molony, and K. Burridge, 1987, J. Biol. Chem. 262, 17,189-17,199) and fragmented by proteolytic digestion. The N-terminal sequences of the intact polypeptide and of several internal peptides were determined and were found to be highly homologous to the mammalian integrin alpha 1-subunit. Monoclonal antibodies to the chick integrin beta 1-chain react on immunoblots with the gizzard integrin beta-subunit (U. Hofer, J. Syfrig, and R. Chiquet-Ehrismann, 1990, J. Biol. Chem. 265, 14,561-14,565). The chain composition of the abundant chick gizzard integrin is therefore alpha 1 beta 1. Polyclonal antibodies to the avian integrin alpha 1-subunit block attachment of embryonic gizzard cells to human and chick collagen IV completely and inhibit attachment to mouse Engelbreth-Holm-Swarm (EHS) tumor laminin partially. In ELISA-style receptor assays, the isolated alpha 1 beta 1 integrin bound to human and chick collagen IV and to mouse EHS tumor and chick heart laminin. While the binding to collagen IV was abolished by removal of divalent cations, the binding to laminin was not sensitive to EDTA under the conditions used. Collagen I bound the isolated avian alpha 1 beta 1 integrin only weakly. As collagen IV was the only extracellular matrix protein for which a consistent, divalent cation-dependent, binding to the avian alpha 1 beta 1 integrin could be demonstrated in both cellular and molecular assays we suggest that it is a preferred ligand for this integrin.     

Analysis of rpsD mutations in Escherichia coli

Summary A certain proportion of protein S7 exists in an altered form in E. coli rpsD (S4) mutants. Depending on the type of S4 mutation involved, two different forms of the altered S7 can be distinguished. The unusual form is longer than normal S7 by about 500 daltons due to extra material at the carboxyl end of the protein. It is suggested that a mutationally altered S4 might lower the efficiency of termination during translation of the messenger for S7. This results in an increased frequency of translational read-through, which gives the observed longer forms of S7. Data are interpreted to mean that one class of S4 mutants might suppress UGA and UAG whereas another class only suppresses UGA.     

Seven new species of Pavonia (Malvaceae) from the Horn of Africa

Pavonia friisii , sp. nov., from south-eastern Ethiopia and south-central and southern Somalia, P. nigrescens , sp. nov., from south-central and southern Somalia, P. matteiana , sp. nov., from south-central Somalia, P. longipilosa , sp. nov., from eastern Ethiopia, P. rotundifolia , sp. nov., from eastern Ethiopia and northern and central Somalia, P. marginata , sp. nov., from central Somalia, and P. paucibracteata , sp. nov., from central Somalia, are described and illustrated.     

SEQ-ED: an interactive computer program for editing, analysis and storage of long DNA sequences

The rapidly growing body of sequenced DNA demands efficientcomputer programs for its analysis and storage. The programdescribed in this paper, SEQ-ED, has been designed to handlea large number of DNA sequences up to 200 kilobases [kb] longstored in a sequence library. In order to minimize the requiredstorage space, the sequences are stored in a compressed formatusing three binary digits per base. In the development of thisprogram, special care has been given to make it easy to usefor molecular biologists without any previous computer experience. Received on September 10, 1984; accepted on October 30, 1984     

Mouse heart laminin. Purification of the native protein and structural comparison with Engelbreth-Holm-Swarm tumor laminin

Laminin was selectively extracted from different mouse tissues using EDTA-containing buffer. By immunoblotting with an antiserum raised against mouse Engelbreth-Holm-Swarm (EHS) tumor laminin, such extracts could be shown to contain laminin-like molecules with a low apparent proportion of A chain to B chains. Native laminin was purified from mouse heart tissue and was shown to have an aberrant polypeptide composition as compared to mouse EHS tumor laminin. Most prominently, mouse heart laminin contains an Mr 300,000 polypeptide which is not antigenically related to the A or the B chains. Furthermore, nonreducible polypeptide components were seen with apparent Mr values of 600,000 and 900,000. The Mr 600,000 component contains epitopes shared with both EHS tumor laminin and the Mr 300,000 polypeptide and possibly represents a covalently cross-linked complex of an A or B chain with the Mr 300,000 chain.