Fibrin : its origin and development in the animal organism, and its relation to life, health, longevity, and disease / by John Goodman.

Date:
1878
Catalogue details

Licence: Public Domain Mark

Credit: Fibrin : its origin and development in the animal organism, and its relation to life, health, longevity, and disease / by John Goodman. Source: Wellcome Collection.

Provider: This material has been provided by the Royal College of Physicians of Edinburgh. The original may be consulted at the Royal College of Physicians of Edinburgh.

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    3. Intense affinities and formative qualities. Blood fibrin, and especially this substance, differs from albumen in possessing intense attractive powers and afanities, which ap- pear to be the secret cause of the formative qualities of fibrin, causing it to form, in definite lines, into rods and substances, &c., which evince the presence of a controlling constructive power, and enable it to assume forms and grotesque figures, of which it might be said, that nothing but vitality was wanting to endow them with the character of living beings. In several instances, the fibrin ah albumen, as we will now call it, mani- fested decided electric attraction, for it was drawn aside and out of its perpendicular, in several instances, some quarter-inch or, so, by attractive influence towards a copper wire when raised from the water. On the other hand, albumen presents itself as a homogeneous, motionless, and shapeless mass, and entirely destitute of these powers and characteristics. 4. Like blood fibrin, it was found to decompose peroxide of hydrogen luitli effervescence, whilst, as stated by Dr. Miller (p. 806), albumen produces no such effect. Again, Dr. Miller tells us, that neutral salts, mixed with blood, on abstraction, prevents its coagulation. This we found to be the case with regard to this substance—even sea-water prevented, in a great measure, the transformation. Is oxygen capable of effecting this change ? Dr. Miller declares (p. 807) that there is a great difference between the action of oxygen on albumen and fibrin. That the former, when exposed to oxygen, enclosed in a glass tube, over mercury, indicates scarcely any absorption of the gas, and little or no carbonic anhydride is eliminated; but when coagulated fibrin is exposed, in a moist state, to the air, it gradually absorbs oxygen, emits carbonic anhydride, and in a few days becomes putrid. I found that fibrin ab albumen as well as blood fibrin, has a great affinity for oxygen, especially when moist and near decomposition ; whilst albumen, in ropes hung up in the atmo- sphere, remained entirely unchanged in its nature, save that it became a brittle rod. In order to show that oxygen of the air takes no part in this transformation (in Exp. 102, 103), I found that the transforma-
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