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Biomedical subjects

A L TAPPEL

Publications and source records attributed to A L TAPPEL.

At least 37 records · Page 2Linked to original sources
PubMed1962

Swelling of fish mitochondria.

The physical properties of fish liver and rat liver mitochondria were compared as a function of temperature and osmotic pressure. The data indicate that fish mitochondria are more flexible and swell at a more rapid rate over a 0 to 30 degrees C temperature range, whereas the rates of swelling at 30 to 40 degrees C are comparable. The swelling rates of both fish and rat mitochondria vary with temperature and approximate the Arrhenius relationship. Apparent energies of activation for swelling averaged 26.5 kcal and 12.9 kcal for rat and fish, respectively. Fish mitochondria were less stable than rat mitochondria to osmotic variation, and the disparity in initial swelling rates became increasingly greater with lower osmotic pressure. The hypotonic swelling of both fish and rat mitochondria was readily reversed osmotically; however, there was a very rapid decay of reversal in fish mitochondria and only a very slow decay in the case of rat. All the data indicate that under comparable conditions the fish mitochondrial membranes are more flexible and presumably more permeable and labile than rat mitochondrial membranes. The findings are discussed in relation to the general metabolic implications and the possible contributions of the membrane constituents to membrane behavior.

Animals↗
PubMed1961

Effect of ionic strength on the kinetics of trypsin and alpha chymotrypsin.

The kinetic effects resulting from changes in the medium ionic strength on reactions involving trypsin or alpha-chymotrypsin are different. The reaction rate increases continuously as the ionic strength increases with alpha-chymotrypsin. With trypsin, the rate increases at low ionic strengths but as the ionic strength further increases a gradual inhibitory effect is observed. The effects produced by different salts of various valence types (from uni-univalent to uni-trivalent or tri-univalent) are essentially the same, and they are a function of the square root of the ionic strength. The quantitative differences among the various salts may be accounted for on the basis of individual properties of the ions, such as the size of the hydrated ion, "association," etc. The effects of salts on the enzymic reactions described herein are amenable to the same electrostatic treatment applicable to non-enzymatic reactions. By applying Brönsted's basic kinetic concepts and the Debye-Hückel law of electrolyte activity, it appears that the salt effects are mainly due to changes in the dissociation of ionizable groups. This appears to be a general method for analyzing the effect of inorganic ions on enzymic reactions.

Chymotrypsin↗