Hammarsten [1872, 1874, 1877] first demonstrated that the rennin action on caseinogen was specific and independent of the action of the calcium salts. His explanation was that the caseinogen molecule was split up into a large molecule (Ruase) and a smaller one (Molkeneiweiss). The "Kiise" was rendered insoluble by the presence of soluble calcium salts and formed the clot. Since then little has ...

1. Enzymically active insoluble derivatives of chymotrypsin and rennin were prepared by coupling each enzyme to agarose as described by Porath, Axén & Ernback (1967) and rennin to aminoethylcellulose by the method of Habeeb (1967). 2. Agarose-chymotrypsin was stable over the range pH2-9, but agarose-rennin released active enzyme into solution at above pH2 and aminoethylcellulose-rennin was simi...

Glycomacropeptide (GMP) is a C-terminal part (f 106-169) of kappa-casein which is released in whey during cheese making by the action of chymosin. GMP being a biologically active component has gained much attention in the past decade. It also has unique chemical and functional properties. Many of the biological properties have been ascribed to the carbohydrate moieties attached to the peptide. ...

Aldosterone quantification helps evaluate the rennin-angiotensin-aldosterone system. The new bead-based multiplex platform has not been applied in aldosterone detection to achieve simultaneous measurements of multiple hormones. A new sensitive competitive bead immunoassay based on Luminex technology for detecting aldosterone in small sample volumes was developed using two-antibody coupled beads...

Children.?By James Burnett, m.d. E. and S. Livingstone, Edinburgh. This small work is intended by the author to serve as an introduction to the subject. As such it seems to fulfil its purpose. Included in the book are separate chapters on the infectious fevers, diseases of the skin, diseases of the nose, throat and ear, and diseases of the eye. These will, doubtless, prove welcome to many. The ...

Aspergillus oryzae has been utilized as a host for heterologous protein production because of its high protein secretory capacity and food-safety properties. However, A. oryzae often produces lower-than-expected yields of target heterologous proteins due to various underlying mechanisms, including degradation processes such as autophagy, which may be a significant bottleneck for protein product...