Glycosaminoglycans were isolated from the equine gastric mucosa. Dowex 1×2 column chromatography was used.
Fractionation of nondialyzable material by Dowex 1×2 column chromatography yielded six fractions at the molarity of NaCl ranging from 0.5 to 2.0mole; they were identified as hyaluronic acid, heparan sulfate, chondroitin-4-sulfate, dermatan sulfate and chondroitin-6-sulfate, respectively.

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Separation and measurement of the third component of complement (C3) and its conversion products in normal human serum can be achieved using the immunofixation electrophoretic technique on agarose gel with the barbltal·lithium·HCl buffer (pH 8.6, μ0.1) firstly proposed by M. Ichimura and T. Baba.
The C3 immunofixation electrophoresis worked well, because utilization of this new buffer was effective on highly clear separation of the β-positioned serum proteins. Consequently, we have resolved native C3 and six C3 conversion products and simultaneously obtained the C3 conversion sequence in serum.
In addition, we are able to measure the concentrations of serum C3 on its conversion products and the C3 biological activities by means of the immunofixation electrophoresis.

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Electrophoretical and biochemical characteristics of amylase in the extracts of lung tissues were investigated.
Amylase activity in the extracts of the diseased lung tissues was significantly higher than in the normal lung tissues. However, electrophoretical properties of amylase in these tissues were revealed to be the same as salivary amylase on polyacrylamide gel electrophoresis.
Heat treatment at 56°C demonstrated that amylase in the extracts of lung tissues was more stable than that of saliva or pancreatic juice.
Amylase activity in saliva and the extracts of lung tissues was suppressed similarly by rabbit antiserum against human salivary amylase.
Km value of amylase in the extracts of lung tissues for Blue Starch was almost same as that of saliva, indicating that both have the same enzymatic nature.

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Hyperferritinemia is often seen in cases of various malignant neoplasms, liver diseases, etc. The results of immunological ferritin assay of patients sera in many diseases revealed that the assay performed using anti-human placental ferritin antiserum gave higher value in malignant neoplasm cases, and that obtained by anti-human liver ferritin antiserum produced higher value in hepatic diseases.
In this paper, we investigated on acidic components of human placental ferritin, the factor which cannot be seen in human liver ferritin with isoelectricfocusing. Immunologically, the antiserum against the acidic components of human placental ferritin showed very higher binding affinity to placental ferritin comparing to liver ferritin. Assay result obtained by this antiserum, absorbed with liver ferritin, revealed that serum ferritin in malignant neoplasms showed higher reactivity but that in liver diseases reacted very little. The immunological assay using this absorbed antiserum was considered to be a little less sensitive but more specific for cancer diagnosis.

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