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Table 3 Hydrodynamic analysis of full-length Myo1c

From: Calmodulin binding to recombinant myosin-1c and myosin-1c IQ peptides

Property

Temperature

Full-length Myo1c

100 μM EGTA

Full-length Myo1c

25 μM CaCl2

Sedimentation coefficient

4°C

25°C

6.70 ± 0.07 S (n = 5)

6.90 ± 0.08 S (n = 4)

  

6.28 ± 0.21 S (n = 8)

*

Stokes radius

4°C

25°C

6.06 ± 0.08 nm (n = 7)

6.07 ± 0.05 nm (n = 4)

  

5.78 ± 0.11 nm (n = 5)

*

Molecular mass

4°C

25°C

168 ± 4 kD

4°C: 173 ± 3 kD

  

150 ± 7 kD

ND

Frictional ratio

4°C

25°C

1.7 ± 0.1

1.7 ± 0.1

  

1.7 ± 0.1

ND

Calmodulins per molecule

4°C

25°C

2.5 ± 0.2

2.9 ± 0.2

  

1.5 ± 0.4

ND

  1. * Very low levels of protein detected.
  2. Full-length Myo1c was co-expressed with calmodulin, purified, and subjected to sucrose-gradient centrifugation or gel-filtration analysis. Myo1c was detected by ELISA (sucrose gradients) or by absorption at 280 nm (gel filtration). Molecular mass was determined using the Stokes-Einstein equation; the number of calmodulins was estimated by subtracting the mass of the Myo1c heavy chain from the estimated molecular mass, then dividing the remainder by the mass of calmodulin (16.7 kD). Values reported are mean ± standard deviation. ND, not determined.