Characteristics of films obtained from fish myofibrillar proteins extracted from various solubilization methods were investigated. In this study, we utilized three agents to solubilize fish myofibrillar proteins from surimi, which are sodium chloride, sodium tripolyphosphate, and alkaline condition. The first part of this study focused on combination of sodium chloride...
A study was completed to determine the extent of the
protein changes occurring in ground beef stored at
2°C for 10 days.
Sections of semitendinosus muscle were obtained
immediately after the slaughter of three beef animals.
Each section was divided into two equal portions, one of
which was ground and...
Investigations were conducted to determine whether the low molecular weight nitrogen compounds and the extra protein complex of bovine psoas major muscle were altered during a 12-day aging period.
Electrophoretic studies of soluble proteins either before or after gel filtration on Sephadex G-25 columns indicated that the soluble proteins were...
The electrophoretic behavior of sarcoplasmic proteins was
investigated by the use of vertical acrylamide gel electrophoresis.
The first part of the study was concerned with the separation of
sarcoplasmic proteins extracted at different times of post-mortem
aging. Electrophoresis of the sarcoplasmic extracts by the discontinuous
technique, using ten percent acrylamide...
An
investigation was
made
into certain
aspects
of
protein
synthesis
at
different
developmental stages
of the
flesh fly
Sarcophaga
bullata.
This
included
measurements
of the
incorporation of
labeled
amino
acids into
protein
by intact cells
from
a
single
organ, the
larval
fat
body,
and
a
study
of
amino
acid
activating...
Cataract is a leading cause of blindness throughout the world, yet the fundamental biochemical causes are unknown. A rodent model of the biochemical processes is selenite cataract. This cataract shows some of the features of human cataracts such as increased lens calcium, proteolysis of proteins, and insolubilization leading to lens...