The binding of iodinated basic fibroblast growth factor (bFGF) to low‐density heparan sulfate proteoglycan purified from the Engelbreth Holm Swarm (EHS) sarcoma was investigated using different techniques. The tumor clearly contained bFGF, the level being comparable to that found in other tissues such as human or bovine brain. 125I bFGF strongly bound to the basement membrane‐like matrix of EHS frozen sections as revealed by autoradiography. Iodinated bFGF bound to purified heparan sulfate proteoglycan but not to laminin or collagen type IV, three components isolated from the same tumor. In contrast, acidic fibroblast growth factor (aFGF) displayed negligible binding to heparan sulfate proteoglycan. Binding of bFGF to frozen sections and to purified proteoglycan could be strongly inhibited by heparin and was displaced by an excess of unlabeled factor and completely suppressed after heparitinase and heparinase treatments. Binding was a function of the salt concentration and was abolished at 0.6 M NaCl. Scatchard analysis indicated the affinity site had a Kd of about 30 nM, a value 10–15 higher than that recently reported by Moscatelli (J. Cell. Physiol., 131:123–130, 1987) in the case of the low‐affinity binding sites present on the surface of baby hamster kidney (BHK) cells.

A systematic study was undertaken to evaluate the urinary Tamm-Horsfall protein (THP), creatinine and total protein elimination in 76 normal subjects divided into five groups during the first 30 years of life. This shows that urinary THP flow, relating to body surface area, increases progressively up to adult age.

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SummaryThe previous demonstration of an association between the collagen-like region of Clq (subcomponent of the first component of complement) and human platelets and of the inhibitory properties of C1q on platelet adhesion and aggregation to or by collagen has led us to consider the first component of complement as a possible modulator of the platelet-collagen interaction. Since collagen represents a major component of the vessel wall, the modification of Cl could play a role in the development of thrombosis.We have therefore studied two patients with abnormalities of complement (low or undetectable C1, C4, C2 and deficiency in C1 inhibitor) who presented with acquired angioneurotic oedema. Both patients had a history of multiple episodes of arterial and/or venous thrombosis.Platelet associated C1q was decreased or undetectable, and this condition was associated with a specific increase of collagen induced aggregation thereby suggesting a possible mechanism for the recurrent thromboembolic episodes.

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Proteins isolated from ribosomal subunits of various mammalian cels were analysed comparatively by two different methods: a two-dimensional polyacrylamide gel electrophoresis system and a recently described two-dimensional immunoelectrophoresis technique. For this purpose, antisera were raised in rabbits against the total mixture of ribosomal proteins from murine cells. These sera were characterized by ring-test, double immunodiffusion and two-dimensional immunoelectrophoresis. They were shown to contain antibodies to a large number of ribosomal proteins. Immunoelectrophoretic analysis of 60S and 40S subunit proteins from rabbit, lamb, canine and human cells using anti-murine sera revealed a striking conservation of their antigenic properties. These results corroborated those obtained by two-dimensional polyacrylamide gel electrophoresis.