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Table 1 Analysis of the individual amino acids involved in the cleavages of elastin

From: Measurement of MMP-9 and -12 degraded elastin (ELM) provides unique information on lung tissue degradation

Hydrophobocity

Amino acid type

Share of elastin*

No. of cleavages in the N-terminal

No. of cleavages in the C-terminal

Percentage of cleavages

R-COOH↓

↓NH2-R

R-COOH↓

↓NH2-R

R-COOH↓

↓NH2-R

Total

Hydrofobic

A

21%

15

30

16

36

14%

29%

21%

P

13%

5

5

4

4

4%

4%

4%

V

12%

5

37

2

12

3%

22%

12%

L

7%

8

5

3

2

5%

3%

4%

I

2%

3

1

<1%

2%

1%

F

2%

4

3

15

2%

8%

5%

Total

57%

    

27%

67%

47%

Hydrophilic

G

28%

71

22

56

33

56%

24%

40%

K

4%

3

21

11%

<1%

5%

S

2%

2

<1%

1%

<1%

Y

2%

1

3

2

<1%

2%

1%

T

2%

1

1

5

<1%

3%

2%

R

2%

4

12

<1%

2%

4%

Q

1%

2

<1%

1%

<1%

Total

43%

    

73%

33%

53%

  1. 114 different peptides were identified. Two cleavage sites (one in the N-terminal and one in the C-terminal) are involved in generating each of these peptides. Each of these cleavage sites involve two amino acids (one cleaved at the NH2-group and the other one at the COOH-group). Arrow () indicates the cleavage site.
  2. *The content of M, E, D, H and C in elastin are ≤1% and not included in the table.