Results 251 to 260 of about 778,605 (292)

Acidic Cysteine Proteinase Inhibitor in Seminal Plasma

Biological Chemistry Hoppe-Seyler, 1985
A cysteine proteinase inhibitor with acidic isoelectric point (pI = 4.7-5.0) was found in human seminal plasma. Its apparent molecular mass is 16 kDa. It inhibits cysteine proteinases like ficin, cathepsin H, cathepsin B and papain. The inhibitory activity of seminal plasma against ficin is almost the same as that of human serum.
K, Minakata, M, Asano
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Caiman Kininogen-Like Cysteine Proteinase Inhibitor

1992
Kininogens are the major mammalian plasma cysteine proteinase inhibitors; a kininogen-like protein was also found in the snake Bothrops jararaca plasma. This communication describes a kininogen-like protein in plasma of Caiman crocodilus vacare. Caiman crude plasma, unlike snake plasma, contains a detectable cysteine proteinase inhibitor. The inhibitor
M S, Araujo, R, Andreotti, A M, Chudzinski, C A, Sampaio, M U, Sampaio   +4 more
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Cystatin S: A Cysteine Proteinase Inhibitor of Human Saliva

The Journal of Biochemistry, 1984
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.
S, Isemura, E, Saitoh, S, Ito, M, Isemura, K, Sanada   +4 more
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Cysteine proteinase inhibitors in elapid and hydrophiid snake venoms

Toxicon, 2002
The ability of elapid and hydrophiid snake venoms to inhibit cathepsin L was tested. All nine species of elapid and three species of hydrophiid snake venoms tested showed inhibition against cathepsin L. All of these venoms tested also showed inhibition against papain as well as against cathepsin L. Among these venoms, two elapid (Laticauda semifasciata
Hiroshi, Mashiko, Hidenobu, Takahashi
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Characterization and Structure of Pineapple Stem Inhibitor of Cysteine Proteinases

Biological Chemistry Hoppe-Seyler, 1992
The complete amino acid sequence of the inhibitor of cysteine proteinases from pineapple stem acetone powder was determined. The inhibitor consists of 52 amino acids and is composed of two polypeptide chains (41 and 11 amino acids) linked via disulphide bonds. It differs from already known sequences in one to four amino acids.
B, Lenarcic, A, Ritonja, B, Turk, I, Dolenc, V, Turk   +4 more
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Cathepsin D inactivates cysteine proteinase inhibitors cystatins

Biochemical and Biophysical Research Communications, 1988
The formation of inactive complexes in excess molar amounts of human cathepsins H and L with their protein inhibitors human stefin A, human stefin B and chicken cystatin at pH 5.6 has been shown by measurement of enzyme activity coupled with reverse-phase HPLC not to involve covalent cleavage of the inhibitors.
B, Lenarcic, J, Kos, I, Dolenc, P, Lucovnik, I, Krizaj, V, Turk   +5 more
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Assay of α-Cysteine Proteinase Inhibitor in Serum or Plasma

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1982
A new proteinase inhibitor has recently been found in human serum or plasma which specifically inhibits cysteine proteinases such as ficin, papain, bromelain and cathepsin B. However, serum contains alpha 2-macroglobulin which also inhibits these cysteine proteinases and, consequently, interferes with the assay of the new alpha-cysteine proteinase ...
K, Minakata, M, Asano, T, Sato, N, Harada   +3 more
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Human cystatin, a new protein inhibitor of cysteine proteinases

Biochemical and Biophysical Research Communications, 1984
A new low-molecular weight protein inhibitor of cysteine proteinases, human cystatin, was isolated from sera of patients with autoimmune diseases. It inhibits papain, human cathepsin H and cathepsin B. According to its partially determined amino-acid sequence, human cystatin is highly homologous to egg white cystatin, but only distantly related to ...
J, Brzin, T, Popovic, V, Turk, U, Borchart, W, Machleidt   +4 more
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Serum α-cysteine proteinase inhibitor levels in pregnancy

Clinical Biochemistry, 1983
Variation in alpha-cysteine proteinase inhibitor levels in human sera were investigated with special attention to the effect of pregnancy and diseases. The inhibitor level in 111 pregnant women, examined by our previous method, increased as the pregnancy advanced.
K, Minakata, M, Asano, H, Mizutani, Y, Kawashima   +3 more
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Cysteine proteinase inhibitors from rabbit skeletal muscle

International Journal of Biochemistry, 1988
1. Two cysteine proteinase inhibitors, I-T (Mr = 29,000) and I-S (Mr = 10,700), were isolated from rabbit skeletal muscle by means of succesive extraction with a neutral buffer solution, precipitation at pH 3.7, acetone fractionation and gel permeation on Sephadex G-75. 2.
M, Matsuishi, A, Okitani, Y, Hayakawa, H, Kato   +3 more
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