Cystatin S: a cysteine proteinase inhibitor of human saliva.

An acidic protein of human saliva, which we named SAP-1 previously, is now shown to be an inhibitor of several cysteine proteinases. The protein inhibited papain and ficin strongly, and stem bromelain and bovine cathepsin C partially. However, it did not inhibit either porcine cathepsin B or clostripain.

[A study on salivary peptide P-C with special reference to intracellular localization of salivary peptide P-C like immunoreactivity in the human pancreatic B-cells].

In order to clarify the intracellular localization of salivary peptide P-C like immunoreactivity in the human pancreatic B-cells, an immuno-electronmicroscopical study using protein A-gold technique was carried out on the human foetal pancreas. Salivary peptide P-C like immunoreactivity was present in some of insulin secretory granules while insulin like immunoreactivity was found in all insulin secretory granules. The finding suggested that new substance in addition to insulin and its precursor was present in the insulin secretory granules of the human pancreatic B-cells.

Isolation and amino acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human gamma-trace.

A low-molecular-weight acidic protein was isolated from human whole saliva by DE32 column chromatography and designated as SAP-1. The amino acid sequence was determined by conventional methods to be (sequence in text). The protein consisted of 113 residues and the calculated molecular weight was 12,552.

Primary structure of cat osteocalcin.

A bone Gla-containing protein (osteocalcin) of cat has been isolated and the complete primary structure has been determined to be YLAPGLGAOAPYPDPLXPKRXICXLNPDCDELADHIGFQDAYRRFYGTV. The protein consists of 49 amino acid residues (Mr. 5,641) containing three Gla residues and a single disulfide bond.

Conformational study of the basic proline-rich polypeptides from human parotid saliva.

The conformational study of two basic proline-rich polypeptides from human parotid saliva, P--D and P--E of known primary structures, was performed by CD and 1H--n.m.r.

[A study on salivary proline-rich peptide P-C with special reference to the presence of salivary peptide P-C in the human respiratory tract].

In order to elucidate whether Salivary Protein C and salivary peptide P-C, originally isolated from human saliva were present in tissues other than those of the salivary glands or not, an indirect immunofluorescence technique using both antisera against salivary peptide P-C and Salivary Protein C was carried out on human salivary glands and the human respiratory tract. As salivary peptide P-C-like immunoreactivity was detected in the serous cells of salivary glands by previous immunohistochemical study, the human respiratory tract was closed as model tissue, since tracheal and bronchial glands in the human respiratory tract consist of mucous and serous cells. Furthermore, to check whether salivary peptide P-C is a fragment of Salivary Protein C or not, the same immunohistochemical study was undertaken on the serial sections of salivary glands and the respiratory tract.

Further fractionation of basic proline-rich peptides from human parotid saliva and complete amino acid sequence of basic proline-rich peptide P-H.

Three basic proline-rich peptides were newly isolated from human parotid saliva, and designated as P-G, P-H, and P-I. The amino acid sequence of P-H was determined to be Ser-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Gln-Gln-Glu-Gly-Asn-Asn- Pro-Gln-Gly-Pro-Pro-Pro-Pro-Ala-Gly-Gly-Asn-Pro-Gln-Gln-Pro-Gln-Ala-Pro-Pro- Ala-Gly-Gln-Pro-Gln-Gly-Pro-Pro-Arg-Pro-Pro-Gln-Gly-Gly-Arg-Pro-Ser-Arg-Pro- Pro-Gln by conventional methods. The amino terminal ten residues of P-H were the same as those of proline-rich peptides P-D, P-E, and P-F reported previously.

[Salivary peptide P-C (III). Its relation to the pathogenesis of diabetes mellitus].

Previous immunohistochemical study showed that salivary peptide P-C like immunoreactivity, originally isolated from whole human saliva, was present not only in human salivary glands but also in human pancreatic B-cells. To elucidate the pathophysiological role of this peptide-like immunoreactivity in human pancreatic B-cells, immunohistochemical study using antisera against both insulin and peptide P-C was carried out on the paraffin embedded pancreatic tissues of 27 diabetic patients and 30 control subjects. Positive immunofluorescence due to insulin was detected in 96% of the diabetic pancreases and 100% of the controls.

Immunohistochemical demonstration of salivary proline rich peptide P-C like immunoreactivity in human pancreatic B-cells.

Antisera against proline rich peptide P-C, recently isolated from human whole saliva were raised in rabbits by injections of peptide P-C-BSA conjugates. Immunohistochemical study using the antisera was carried out on human salivary glands, gut and pancreas. The results showed that peptide P-C like immunoreactivity was present not only in the salivary glands but also in the pancreatic islets, though not in the gut.

Complete amino acid sequence of a basic proline-rich peptide, P-F, from human parotid saliva.

The complete amino acid sequence of a basic proline-rich peptide, P-F, isolated from human parotid saliva was determined to be Ser-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Gly-Asn-Gln-Pro-Gln-Gly-Pro-Pro-Pro-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Asn-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Pro-Gly-Lys-Pro-Gln-Gly-Pro-Pro-Pro-Gln-Gly-Ser-Lys-Ser-Arg-Ser-Ala by conventional methods. P-F contains a number of repeating sequences and oligo-proline structures identical with those in other proline-rich peptides such as P-C, P-D, P-E, and Protein C. P-F has the highest degree of homology with P-E among these proline-rich peptides.

Amino acid sequences of glycopeptides obtained from basic proline-rich glycoprotein of human parotid saliva.

A proline-rich glycoprotein, in which proline, glutamic acid, and glycine represent about 80 per cent of the total residues, was obtained from human parotid saliva. The amino acid sequences of glycopeptides obtained from digests of the glycoprotein with clostripain were determined to be Pro-Gly-Lys-Pro-Glu-Gly-Pro-Pro-Pro-Gln-Gly-Gly-Asn(CHO)-Gln-Ser-Gln-Gly-Pro- Pro-Pro-Arg and Pro-Pro-Gln-Gly-Gly-Asn(CHO)-Gln-Ser-Gln-Gly-Pro-Pro-Pro-His-Pro-Gly-Lys-Pro -Glu-Arg. The structural relationship between the glycopeptides and the known salivary peptide is discussed.

Conformational study of the salivary proline-rich polypeptides.

The conformational study of three proline-rich polypeptides of human whole saliva, with known primary structures, was performed by CD and 1H-n.m.r.

[The presence of proline-rich peptide P-C like immunoreactivity in the human pancreatic B-cells].

It is well known that there are functional and morphological similarities between the salivary glands and the pancreas. Amylase, kallikrein and glucagon are present in both tissues. Morphological similarities of the two tissues have been observed by using a light and electron microscope.

Organic acids and branched-chain amino acids in body fluids before and after multiple exchange transfusions in maple syrup urine disease.

We successfully treated a critically ill infant with the classical type of maple syrup urine disease by multiple exchange transfusions via a peripheral artery and vein and with positive calorie supplementation in the early stage of therapy. Clinical improvement was definite after the plasma leucine level fell below 1 mmol/l. There was a close linear correlation between plasma concentrations of branched-chain amino acids and their corresponding branched-chain alpha-keto acids and branched-chain alpha-hydroxy acids.