Læknablaðið : fylgirit - 01.05.1978, Blaðsíða 145

TABLE II
AMINO ACID COMPOSITION OF VOXD VOLUM^
MATERIALS OBTAINED FROM AMYLOID—LADEN AND
NORMAL HUMAN TISSUE.
Residues per 100
Amyloid Vg-material Normal tissue Vp-material
T.H. Liver Normal Liver
Asp 9.1 9.4
Thr 5.2 5.2
Ser 7.1 7.9
Glu 12.4 12.8
Pro 5.7 5.0
Gly 9.1 8.7
Ala 7.4 7.1
>sCys 1.8 1.7
Val 5.4 5.7
Met 2.1 2.1
Ile 3.9 4.1
Leu 8.7 9.1
Tyr 2.6 3.1
Phe 6.6 4.5
His 2.1 2.1
Lys 5.8 6.6
Arg 5.3 5.0
where the only significant difference is in the
content of phenylalamine.
Antigenic similarities between amyloid fibrils
and normal organ preparations was also observed.
Thus the normal tissue extract reacted identi-
cally with both crude amyloid fibrils and amy-
loid V0-material when tested againstan antiserum
to amyloid V0-material (Fig. 3).
Pras and Glynn (15) have reported a material
similarly obtained from pig kidney and liver.
They suggested this material to be a retieulin
protein. Also this material was very similar
in its amino acid composition to the amyloid
V0-materials studied by us. It is thus conceiv-
able that also the VQ-material of amyloid is a
connective tissue protein.
In conclusion: It is suggested that both of
the two major proteins of secondary amyloid
fibrils are derived from connective tissue, which
is highly involved in the chronic inflammation,
seen in rheumatic diseases.
Fig. 3 Double diffusion in agarose. Anti-
amyloid Vo-material in central well
tested against crude DAM from T.H.
liver (1), crude water extract from
normal liver treated with 0.1 N NaOH
(2), amyloid Vo-material (3), and Vo-
material from normal liver (4). The
other peripheral wells are filled with
saline.
R eferences:
1. Anders, R.F. , Natvig, J.B. , Miehaelsen,
T.E. & Husby, G. Isolation and characteriza
tion of amyloid-related serum protein SAA
as a low molecular weight protein. Scand,
J. Immunol. 4 , 397, 1975.
2. Benditt, E.P. , Cohen, A.S. , Franklin,
E.F., Glenner, G.G., Husby, G., Natvig,
J.B., Osserman, E. F. and Wegelius, O.
Nomenclature for amyloid proteins and
related serum components. In Amyloidosis,
eds. O. Wegelius and A. Pasternack.
Academic Press, New York, London, In
press.
3. Benditt, E.P. , Eriksen, N. , Hermodson,
M.A. & Eriesson, L.H. The major
proteins of human and monkey amyloid
substances: Common properties including
unusual N-terminal amino acid sequences.
FEBS Letters 19,169, 1971.
4. Cohen, A.S. & Calkins, E. Electron
microscopic observations on fibrons
components in amyloid of different organs.
Nature (Lond.) 183, 1202, 1959.
5. Ein, D., Kimura, S & Glenner, G.G. An
amyloid fibril protein of unknown origin:
Partial amino acid sequence analysis.
Biochem. Biophys. Res. Comm. 46, 498,
1972.
143