Correction: Specific Covalent Binding of Platelet-Derived Growth Factor to Human Plasma a2-MacroglobulinSource: Proceedings of the National Academy of Sciences of the United States of America,Vol. 81, No. 8, [Part 1: Biological Sciences] (Apr. 15, 1984), p. 2586Published by: National Academy of SciencesStable URL: http://www.jstor.org/stable/23598 .

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2586 Corrections Proc. Natl. Acad. Sci USA 81 (1984)

Correction. In the article "Specific covalent binding of plate- let-derived growth factor to human plasma a2-macroglobu- lin" by Jung San Huang, Shuan Shian Huang, and Thomas F. Deuel, which appeared in number 2, January 1984, of Proc. Natl. Acad. Sci. USA (81, 342-346), the printer omit- ted the arrow in Fig. 3B indicating the position of a2-macro- globulin. A correct Fig. 3 is reproduced here.

B

2.8 A

2.4

o l B -

0

1.6 193 189 186 183 179 176 173 169 166 163 z 1.2c

0

<0.8 .4

0.4-

0 120 160 200 240 280 320 FRACTION NUMBER

193 189 186 183 119 176 173 169 166 163

FIG. 3. (A) Chromatographic profile of polyethylene glycol precipitates of human plasma on Ultrogel AcA34/Ultrogel AcA22. Human plasma (88 ml) was precipitated at 5.5-12.5% (wt/vol) polyethylene glycol as described by Barrett (23). The precipitates were dissolved in 20 ml of 0.1 M sodium citrate (pH 6.0) and then applied onto a column (5.0 x 72 cm) of Ultrogel AcA34/Ultrogel AcA22, 2:1 (vol/vol), and eluted with the same buffer. The flow rate and fractional volume were 20 ml/hr and 3 ml, respectively. The second protein peak from fractions 155-170 was identified as a2M by trypsin assay and by immunodiffusion. The purity of a2M obtained from the main fractions of the second protein peak is >95%. The a2M obtained only showed the slow form after electrophoresis in pore-limiting polyacrylamide gels. (B and C) NaDodSO4/poly- acrylamide gel Coomassie brilliant blue staining patterns (B) and autoradiographs (C) of the fractions from 2:1 Ultrogel AcA34/Ultrogel AcA22 column chromatography after reaction with 125I-PDGF. Each fraction (100 Al from fraction 163 to fraction 193) was incubated with 100 ng of 1251-PDGF. After incubation at room temperature for 30 min, 6 ,ul of the reaction mixture was analyzed with NaDodSO4/PAGE (5% gel) followed by autoradiography. The arrows shown in (B) and (C) indicate the locations of a2M and the 25I-PDGF-a2M complex, respectively. A smaller percentage of 125I-PDGF complexes with a2M formed at pH 6.0; the optimal pH for complexation of 125I-PDGF to a2M is 7.4.

Correction. In the article "Increasing the intracellular Na+ concentration induces differentiation in a pre-B lymphocyte cell line" by Philip M. Rosoff and Lewis C. Cantley, which appeared in number 24, December 1983, of Proc. Natl. Acad. Sci. USA (80, 7547-7550), the following corrections should be noted. On page 7547, the first line of the right-hand column should read "fetal calf serum (GIBCO)/10 ,uM Na pyruvate/10 mM Hepes." On page 7548, the second line of the legend to Table 1 should read ". . . was used at a final concentration of 400 ,tM...."

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