238
SILVIO RANZI
monium sulphate concentration (Figs. 28 and 29). We conclude therefore that the difference in the salting-out diagrams of embryos treated
with NaSCN, IBA or LiCl probably originates from the physico-chemical
conditions of their proteins and not from the synthesis of new protein
fractions.
40
30
l-O
X
Ik
2
°
10
00
10 20 30 40 50 60 70 C
FIG. 29. Salting-out diagram for hen egg lipovitellin: IBA- and NaSCN-treated protein
compared with normal protein.
C. Animalizing Agents Denaturing Proteins
In early research work in this field (Arosio, Citterio, Menotti, Ranzi
and Semenza, 1946) it was possible to demonstrate that animalizing
agents induce a decrease in viscosity of solutions of protein particles
which under viscosimetric analysis appear fibrillar or folded fibrillar.
The vegetalizing agents induce instead an increase in viscosity of the
same protein solutions. These changes in viscosity (Fig. 30) are related
to the shape of the particles in solution because they appear only in
solutions containing fibrillar or folded fibrillar proteins and not in solutions of globular proteins (Citterio and Ranzi, 1947). Both animalizing
and vegetalizing agents induce an increase in viscosity of the globular
protein solutions. The importance of the observed differences in action
of animalizing and vegetalizing substances on fibrillar, or folded fibrillar,
proteins has been apparent since the early stages of this research.
Viscosimetric data on the action of animalizing agents on globular
protein solutions (increasing viscosity) and on fibrillar or folded fibrillar
protein solutions (decreasing viscosity) suggests a protein denaturation.
This denaturation, by breaking some bonds, increases the volume of
o
o Contr.
• — - I B A
' \
-—- NaSCN
SILVIO RANZI
monium sulphate concentration (Figs. 28 and 29). We conclude therefore that the difference in the salting-out diagrams of embryos treated
with NaSCN, IBA or LiCl probably originates from the physico-chemical
conditions of their proteins and not from the synthesis of new protein
fractions.
40
30
l-O
X
Ik
2
°
10
00
10 20 30 40 50 60 70 C
FIG. 29. Salting-out diagram for hen egg lipovitellin: IBA- and NaSCN-treated protein
compared with normal protein.
C. Animalizing Agents Denaturing Proteins
In early research work in this field (Arosio, Citterio, Menotti, Ranzi
and Semenza, 1946) it was possible to demonstrate that animalizing
agents induce a decrease in viscosity of solutions of protein particles
which under viscosimetric analysis appear fibrillar or folded fibrillar.
The vegetalizing agents induce instead an increase in viscosity of the
same protein solutions. These changes in viscosity (Fig. 30) are related
to the shape of the particles in solution because they appear only in
solutions containing fibrillar or folded fibrillar proteins and not in solutions of globular proteins (Citterio and Ranzi, 1947). Both animalizing
and vegetalizing agents induce an increase in viscosity of the globular
protein solutions. The importance of the observed differences in action
of animalizing and vegetalizing substances on fibrillar, or folded fibrillar,
proteins has been apparent since the early stages of this research.
Viscosimetric data on the action of animalizing agents on globular
protein solutions (increasing viscosity) and on fibrillar or folded fibrillar
protein solutions (decreasing viscosity) suggests a protein denaturation.
This denaturation, by breaking some bonds, increases the volume of
o
o Contr.
• — - I B A
' \
-—- NaSCN