No abstract

1) Cold pack therapy produces significant temperature falls in cutaneous and subcutaneous superficial tissues without directly changing the temperature of tissues at or more than 2.0 cm below the skin; and 2) the temperature gradients of both layers of tissue reverses after treatment, indicating that the deep tissue beneath is at least one of the sources of heat used to rewarm the cooled superficial tissue. The latter finding underscores the importance of the hemodynamic interchange between superficial and deep tissues, and offers an explanation for the reduction of pain, muscle spasm, and edema observed with cold therapy in several clinical situations.

Myosin, fibrinogen and albumin gels were formed by heating in pH 6.0 phosphate buffer at three heating rates. Turbidity (Ahben,,,) and solubility were monitored along with gel strength, as measured with an annular pump. Myosin and fibrinogen suspensions became turbid and solubility decreased as temperatures preceding the development of gel strength. Linearly increasing heating rates of I2"C/hr and 5O"Ci hr produced the strongest myosin and fibrinogen gels at 7O"C, whereas albumin gels formed at 95°C by heating at 12Whr or constant heating for 20 min did not differ in strength.

The proteolytic activity of ginger rhizome was studied with bovine serum albumin (BSA), collagen and actomyosin as substrates. A semipurified, powdered enzyme preparation was prepared by buffer extraction of an acetone powder of ginger rhizome and subsequent acetone precipitation of the proteolytic principle from the buffer extract. With 3% BSA as substrate, a relatively high proteolytic activity occurred over a pH range of 4.5–6.0, with an optimum pH of 5.0. The optimum temperature for proteolysis of BSA was 60°C during a 10 min reaction time, with rapid denaturation of the enzyme occurring at 70° C. NaCl in cone up to 10% produced about a 20 and 50% reduction in proteolysis of collagen and BSA, respectively. The ginger protease was protected by dithiothreitol during extraction and reaction, indicating the involvement of −SH groups at the active site. The analyses of soluble peptide amino acids or terminal amino acids suggest that the proteolysis of collagen is many fold greater than that of actomyosin. The combined proteolysis of these two muscle protein fractions by the ginger protease resulted in significantly more tender meat. According to conventional nomenclature, “Zingibain” is the proper name for this proteolytically active principle in Zingiber officinale roscoe or ginger rhizome which is commonly referred to as gingerroot. For meat applications, a possible advantage of zingibain over papain and ficin is the greater proteolysis of collagen in comparison to actomyosin. When compared to reported values for bromelain, zingibain has a higher optimum activity temperature, which is desirable in some applications

From this the largest published comprehensive cohort of IBMFSs, it can be concluded that recent advances have led to successful genotyping of about half of the patients. Establishing a genetic diagnosis is still challenging and there is a critical need to develop novel diagnostic tools.