Spleen lysozyme

An autoradiographic study has been made of the distribution of I-labelled lysozyme after its intravenous injection in rats. As part of a study on structure-activity relationships of mammalian tissue lytic enzymes, the location and characterization of multiple forms of rat kidney lysozyme have been reported. Iron-deficient rats have been shown to have higher levels of kidney lysozyme activity than control animals. There were no significant changes in the serum and spleen lysozyme activity levels in iron deficiency. 

The Pro content of five a-lactalbumins is two residues per molecule the remainder (with the exception of rat) are also low in Pro (one to three residues). Most of the hen egg-white lysozymes have two Pro residues, the remaining egg white and mammalian lysozymes ranging from one to five residues (except canine spleen). 

The acid phosphatases include all phosphatases that hydrolyze phosphate esters with an optimum pH of less than 7.0. They are present in the lysozymes of the secretory epithelial cells. Although acid phosphatase is produced primarily by the prostate gland, it is also found in erythrocytes, platelets, leukocytes, bone marrow, bone, liver, spleen, kidney, and intestine. 

Lysozyme of mink spleen, kidneys, and liver has been isolated by affinity chromatography on deaminated chitin. The L-histidine content of the enzyme was unusually high. The lysozyme preparations contained an unknown, firmly bound component which absorbed at 400—420 nm. 

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