Snow Brand Milk Products Co., Ltd.

Yasuharu Itagaki

Kanji Higashio

Morimasa Tanimoto

Nobuyuki Shima

Shinjiro Mitsuda

Seiji Kurosawa

Masaya Nagao

Mio Imamura

Akira Suzuki

Hidetoshi Ishikawa

Taisuke Iwasaki

Jan Sikkema

Klaas Doesburg

Tetsuro Ohba

The new glycoprotein, which possesses an anti-tumor activity, a leukemia cell differentiation inducing activity, a cellular immunology enhancing activity, a vascular endothelial cell growth stimulating activity and a hepatocyte growth stimulating activity, can be obtained.

Human-derived glycoprotein, biologically active factor which includes glycoprotein, and pharmaceutical product which comprises biologically active factor as active component

A novel primer is provided which is useful in the reverse transcription polymerase chain reaction to amplify &agr;,-casein gene and keratin gene contained in milk. A method is also provided for using the expression ratio of their genes to examine the pathological conditions of mammalian mastitis or determine the milk protein synthesis level in mammary gland cells. The method is quick and accurate and avoids the need for excising mammary gland tissue.

Method for determining mastitis using keratin and casein which are amplified by primers

The present invention relates to a method of synchronizing epithelial cells into G.sub.0 phase, more specifically, a method of synchronizing epithelial cells into G.sub.0 phase characterized by culturing the cells in a synthetic medium for 5 days or more, wherein said synthetic medium is a medium with the lowered concentration of bovine fetal serum 5% or less and said epithelial cells is bovine mammary gland cells. Further, the present invention relates to a method of culturing cells characterized by using G.sub.0 phase synchronized cells obtained by the present invention, and a method of screening a related to differentiation and/or maturation of said cells by using G.sub.0 phase synchronized cells. The present invention is useful for easily synchronizing epithelial cells into G.sub.0 phase and for screening a factor related to differentiation and/or maturation of epithelial cells.

Method of synchronizing epithelial cells into G.sub.0 phase

This invention provides compositions for fair-skin containing the phosphorylated polysaccharides produced by lactic acid bacteria as an effective ingredient. The phosphorylated polysaccharides are expressed, for example, by the following formula and contained in the compositions for fair-skin at concentrations of 0.01-20 weight % and are used such as creams, emulsions and toilet lotions. The compositions for fair-skin exhibit fair-skin effect by inhibiting activities to melanoma proliferation and melanin formation. ##STR1## (wherein, Glc, Gal and Rha represent glucose, galactose and rhamnose residues, respectively. Numerals shown by other than subscript represent the respective binding sites and n represents the degree of polymerization of 1,000-5,000).

Compositions for fair-skin

A whitening cosmetic preparation containing angiogenin as an effective component is disclosed. Angiogenin used in the present invention may be derived from milk, especially bovine milk. The whitening cosmetic preparation contains at least 0.001% by weight, preferably from 0.01 to 20% by weight angiogenin based on the total amount of said preparation. A method for whitening skin comprising administration of angiogenin to skin is also disclosed. The whitening cosmetic preparation inhibits melanin production and prevents the developments of blotches and freckles of skin.

Whitening cosmetic preparation and method of using same

Human derived glycoprotein, biologically active factor which includes

A novel tissue plasminogen activator having the following characteristics: molecualr weight of 65,000-72,000 Daltons as measured by SDS-PAGE electrophoresis using at 7.5% agarose gel; plasminogen activator specific activity of about 10.4.times.10.sup.4 IU/mg, wherein specific activity is defined as the ratio of fibrinolytic activity of purified t-PA measured on fibrin-agarose plates to milligrams of protein; about 83.1% absorption of t-PA by a fibrin-Sepharose column when applied; binds to a Concanavalin A column when applied; the fibrinolytic activity is substantially undiminished by heating at 60.degree. C. for 60 minutes or 95.degree. C. for 5 minutes relative to unheated t-PA; unreactive with polyclonal antisera raised against urokinase; the fibrinolytic activity is substantially stable at pH 5-10; exhibits fibrinolytic activity at pH 7.5-9.0 and temperature 39.degree.-41.degree. C.; a Km value of about 1.16.times.10.sup.-3 mol/liter and a V.sub.max of about 11.7.times.10.sup.-8 mol/liter for substrate S-2288; and fibrinolytic activity is inhibited by Co.sup.2+ Zn.sup.2+, Cd.sup.2+, Hg.sup.2+, Ni.sup.2+ and Cu.sup.2+.

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Tochigi, Japan

Yasuharu Itagaki