Isolation of a low-molecular-weight serum component antigenically related to an amyloid fibril protein of unknown origin.

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

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BIOCOLLOIDS IN NORMAL HUMAN URINE: II. PHYSICOCHEMICAL AND IMMUNOCHEMICAL CHARACTERISTICS

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y58-127 ◽

1958 ◽

Vol 36 (1) ◽

pp. 1167-1175 ◽

Cited By ~ 1

Author(s):

T. Webb ◽

B. Rose ◽

A. H. Sehon

Keyword(s):

Molecular Weight ◽

Normal Serum ◽

Low Molecular Weight ◽

Free Diffusion ◽

Albumin Fraction ◽

Serum Component ◽

Normal Human ◽

Normal Urine ◽

Immunochemical Characteristics ◽

Serum Components

The biocolloids of normal urine were separated by electrophoresis on starch and compared with similarly prepared fractions of serum by ultracentrifugal, free diffusion, and immunochemical techniques. The albumin fraction of urine was indistinguishable from the serum component. The urinary γ2-globulins were shown to consist of low molecular weight (10,000) fragments of the normal serum components. The other globulins of the urine were antigenically related to some of the serum components but appeared to contain lower molecular weight materials. Some of the components of normal serum could not be detected in the urine and the urine contained at least two components which were not present in the serum.

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Amino Acid Sequence of an Amyloid Fibril Protein of Unknown Origin

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)81154-5 ◽

1972 ◽

Vol 247 (17) ◽

pp. 5653-5655 ◽

Cited By ~ 1

Author(s):

Daniel Ein ◽

Shigeru Kimura ◽

William D. Terry ◽

Judith Magnotta ◽

George G. Glenner

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Amyloid Fibril ◽

Unknown Origin ◽

Amyloid Fibril Protein

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An amyloid fibril protein of unknown origin: Partial amino-acid sequence analysis

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(72)80166-9 ◽

1972 ◽

Vol 46 (2) ◽

pp. 498-500 ◽

Cited By ~ 34

Author(s):

D. Ein ◽

S. Kimura ◽

G.G. Glenner

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Amyloid Fibril ◽

Unknown Origin ◽

Amino Acid Sequence Analysis ◽

Partial Amino Acid Sequence ◽

Amyloid Fibril Protein

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A high-performance oil-free backing pump for electron microscopes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100107691 ◽

1978 ◽

Vol 36 (1) ◽

pp. 110-111

Author(s):

G.K.W. Balkau ◽

E. Bez ◽

J.L. Farrant

Keyword(s):

Molecular Weight ◽

Electron Microscope ◽

Hot Spots ◽

High Performance ◽

Carbonaceous Material ◽

Contamination Rate ◽

Low Molecular Weight ◽

Principal Source ◽

Rotary Pumps ◽

Electron Microscopes

The earliest account of the contamination of electron microscope specimens by the deposition of carbonaceous material during electron irradiation was published in 1947 by Watson who was then working in Canada. It was soon established that this carbonaceous material is formed from organic vapours, and it is now recognized that the principal source is the oil-sealed rotary pumps which provide the backing vacuum. It has been shown that the organic vapours consist of low molecular weight fragments of oil molecules which have been degraded at hot spots produced by friction between the vanes and the surfaces on which they slide. As satisfactory oil-free pumps are unavailable, it is standard electron microscope practice to reduce the partial pressure of organic vapours in the microscope in the vicinity of the specimen by using liquid-nitrogen cooled anti-contamination devices. Traps of this type are sufficient to reduce the contamination rate to about 0.1 Å per min, which is tolerable for many investigations.

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