Biomedical Engineering Reference
In-Depth Information
125
Iodine decay table
Table 6.6.
Days
Number
Days
Number
Days
Number
−10
1.122
24
0.758
58
0.512
−8
1.097
26
0.741
60
0.500
−6
1.072
28
0.724
62
0.489
−4
1.047
30
0.707
64
0.477
−2
1.023
32
0.691
66
0.467
0
1.000
34
0.675
68
0.456
2
0.977
36
0.660
70
0.445
4
0.955
38
0.645
72
0.435
6
0.933
40
0.630
74
0.426
8
0.912
42
0.616
76
0.416
10
0.891
44
0.602
78
0.406
12
0.871
46
0.588
80
0.397
14
0.851
48
0.574
82
0.388
16
0.831
50
0.561
84
0.379
18
0.812
52
0.548
86
0.370
20
0.794
54
0.536
88
0.362
22
0.776
56
0.524
90
0.354
If started with 15 kBq
32
P, 1 5
=
a)
·
0.787
11.805 kBq are present
Examples
5 days later.
When 8000 dpm
32
P are measured at day 6, the sample originally
contained 8000
b)
/
=
0.748
10 695 dpm and 178.25 Bq.
6.3 Enzymatic [
32
P]-Phosphate Incorporation
into Proteins
A lot of biologic membrane systems and cellular organelles contain
Chemical stability
of amino acid
phosphates
kinases, which transfer phosphate groups to proteins, especially
to serine, threonine, and tyrosine residues. Self-phosphorylation
of enzymes leading to acylphosphates or phosphoamides can be
observed, too. With respect to their chemical stability, these phos-
phoproteins are classified into acid-stable (alkali labile), hydroxyl-
amine-sensitive, and acid labile.
References
Weller M (1979) Protein phosphorylation: the nature, function, and
metabolism of proteins with covalently bound phosphorus. Pion, Lon-
don
The catalytic subunit of the cycloAMP-dependent protein kinase
(cAMP PrK) transfers the terminal (
γ
) phosphate residue of ATP to
serine residues of numerous proteins. The assay described in this
